| blob | 50aff8a973821753534ea36d93b39154dacad187 |
1 ID GCDH_CAEEL Reviewed; 409 AA.
2 AC Q20772;
3 DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
4 DT 01-NOV-1996, sequence version 1.
5 DT 31-OCT-2006, entry version 47.
6 DE Probable glutaryl-CoA dehydrogenase, mitochondrial precursor
7 DE (EC 1.3.99.7) (GCD).
8 GN ORFNames=F54D5.7;
9 OS Caenorhabditis elegans.
10 OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
11 OC Rhabditidae; Peloderinae; Caenorhabditis.
12 OX NCBI_TaxID=6239;
13 RN [1]
14 RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
15 RC STRAIN=Bristol N2;
16 RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
17 RG The C. elegans sequencing consortium;
18 RT "Genome sequence of the nematode C. elegans: a platform for
19 RT investigating biology.";
20 RL Science 282:2012-2018(1998).
21 CC -!- CATALYTIC ACTIVITY: Glutaryl-CoA + acceptor = crotonoyl-CoA +
22 CC CO(2) + reduced acceptor.
23 CC -!- COFACTOR: FAD (By similarity).
24 CC -!- PATHWAY: Degradative pathway of L-lysine, L-hydroxylysine, and L-
25 CC tryptophan metabolism.
26 CC -!- INTERACTION:
27 CC P39745:mpk-1; NbExp=1; IntAct=EBI-313068, EBI-321013;
28 CC Q17446:pmk-1; NbExp=1; IntAct=EBI-313068, EBI-312987;
29 CC -!- SUBCELLULAR LOCATION: Mitochondrion; mitochondrial matrix
30 CC (Potential).
31 CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
32 CC -----------------------------------------------------------------------
33 CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
34 CC Distributed under the Creative Commons Attribution-NoDerivs License
35 CC -----------------------------------------------------------------------
36 DR EMBL; Z66513; CAA91333.1; -; Genomic_DNA.
37 DR PIR; T22647; T22647.
38 DR UniGene; Cel.30446; -.
39 DR HSSP; Q06319; 1BUC.
40 DR IntAct; Q20772; -.
41 DR Ensembl; F54D5.7; Caenorhabditis elegans.
42 DR KEGG; cel:F54D5.7; -.
43 DR WormBase; WBGene00010052; F54D5.7.
44 DR WormPep; F54D5.7; CE03411.
45 DR GO; GO:0005515; F:protein binding; IPI:IntAct.
46 DR InterPro; IPR006089; Acyl_CoA_DH.
47 DR InterPro; IPR006091; Acyl_CoA_DH/ox_M.
48 DR InterPro; IPR006090; Acyl_CoA_DH_1.
49 DR InterPro; IPR006092; Acyl_CoA_DH_N.
50 DR InterPro; IPR009075; AcylCo_DH/ox_C.
51 DR InterPro; IPR013786; AcylCoA_DH/ox_N.
52 DR InterPro; IPR009100; AcylCoA_DH/ox_NM.
53 DR InterPro; IPR013764; AcylCoA_DH_1/2_C.
54 DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
55 DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
56 DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
57 DR PROSITE; PS00072; ACYL_COA_DH_1; FALSE_NEG.
58 DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
59 KW Complete proteome; FAD; Flavoprotein; Hypothetical protein;
60 KW Mitochondrion; Oxidoreductase; Transit peptide.
61 FT TRANSIT 1 ? Mitochondrion (Potential).
62 FT CHAIN ? 409 Probable glutaryl-CoA dehydrogenase.
63 FT /FTId=PRO_0000000530.
64 FT ACT_SITE 388 388 Proton acceptor (Potential).
65 SQ SEQUENCE 409 AA; 44964 MW; 4D06241FB6768069 CRC64;
66 MLTRGFTSIG KIASRGLSST FYQDAFQLSD QLTEDERSLM LSAREYCQER LLPRVTEAYR
67 TEKFDPSLIP EMGSMGLLGA PYQGYGCAGT STVGYGLIAR EVERVDSGYR STMSVQTSLV
68 IGPIYNYGSE DQKQKYIPDL ASGKKIGCFG LTEPNHGSNP GGMETKATWD ETTKTYKLNG
69 SKTWISNSPV SDVMVVWARS ARHNNKIKGF ILERGMKGLT TPKIEGKLSL RASITGQIAM
70 DDVPVPEENL LPNAEGLQGP FGCLNNARLG IAWGALGAAE ECFHLARQYT LDRQQFGRPL
71 AQNQLMQLKM ADMLTEISLG LQGCLRVSRL KDEGKVQSEQ ISIIKRNSCG KALEVARKAR
72 DMLGGNGIVD EYHIMRHMVN LETVNTYEGT HDVHALILGR AITGLNGFC
73 //
74 ID Q41V66_FERAC Unreviewed; 607 AA.
75 AC Q41V66;
76 DT 27-SEP-2005, integrated into UniProtKB/TrEMBL.
77 DT 27-SEP-2005, sequence version 1.
78 DT 31-OCT-2006, entry version 6.
79 DE Glycoside hydrolase, family 15.
80 GN ORFNames=FaciDRAFT_1685;
81 OS Ferroplasma acidarmanus Fer1.
82 OC Archaea; Euryarchaeota; Thermoplasmata; Thermoplasmatales;
83 OC Ferroplasmaceae; Ferroplasma.
84 OX NCBI_TaxID=333146;
85 RN [1]
86 RP NUCLEOTIDE SEQUENCE.
87 RC STRAIN=Fer1;
88 RG US DOE Joint Genome Institute (JGI-PGF);
89 RA Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina T.,
90 RA Hammon N., Israni S., Pitluck S., Richardson P.;
91 RT "Sequencing of the draft genome and assembly of Ferroplasma
92 RT acidarmanus fer1.";
93 RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
94 RN [2]
95 RP NUCLEOTIDE SEQUENCE.
96 RC STRAIN=Fer1;
97 RG US DOE Joint Genome Institute (JGI-ORNL);
98 RA Larimer F., Land M.;
99 RT "Annotation of the draft genome assembly of Ferroplasma acidarmanus
100 RT fer1.";
101 RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
102 RN [3]
103 RP NUCLEOTIDE SEQUENCE.
104 RC STRAIN=Fer1;
105 RG US DOE Joint Genome Institute (JGI-PGF);
106 RA Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina T.,
107 RA Hammon N., Israni S., Pitluck S., Richardson P.;
108 RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
109 CC -!- CAUTION: The sequence shown here is derived from an
110 CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
111 CC preliminary data.
112 CC -----------------------------------------------------------------------
113 CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
114 CC Distributed under the Creative Commons Attribution-NoDerivs License
115 CC -----------------------------------------------------------------------
116 DR EMBL; AABC04000001; EAM94575.1; -; Genomic_DNA.
117 DR GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:InterPro.
118 DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
119 DR GO; GO:0005976; P:polysaccharide metabolism; IEA:InterPro.
120 DR InterPro; IPR008928; 6hp_glycosidase.
121 DR InterPro; IPR011613; Glyco_hydro_15_rel.
122 DR InterPro; IPR012343; Glyco_trans_sub.
123 DR Pfam; PF00723; Glyco_hydro_15; 1.
124 KW Hydrolase.
125 SQ SEQUENCE 607 AA; 69495 MW; 8AC6297BA16ED500 CRC64;
126 MGTYRGLYDL HDAYRSDYLK IANHGFIANN RTAALVGIDG TIDWACLPNF NSNPVFDSIL
127 DARNGGYFKT SPVMESNVNQ YYEESTNILI TEFVNNNQVI LRLTDFLPTS SYSTITFPEI
128 HRLIEAPYSD VEVSIDIKSH FNFGSGKTNI TRDRNGYIFS CTDDTLGIST NLKLKKGNGN
129 VYSRIKVEKG SHEWIVVLSG VRQIGNVRQY ESYTRLEETR NYWSAWAGKI NYSGLYYDHV
130 IRSALTLRGL FYDPTGMMVA APTTSLPEII GGERNWDYRY TWIRDTAYVV EALSLIGLND
131 VATKFLYDIM SIVQKDKKVK TIYPVNGDSK LEEKKVNLSG YMDSIPVRIG NEASEQLQID
132 QYGSIVNAVF RFHEAGGLVT TYLWDFLIEI LDTLKDIWKL PDSSIWEFRS EPKHYLYSKL
133 ISWSAFNRAI KMGRELGYSA PYRTWHKIRE EIKNEIMEKG YNPDVKAFTQ YYGSDQMDAS
134 VLRMPLTGII SAKDPRFVST LARVEAELKN PCGMFIRYHS DDGLKGHDNA FLLLSFWYVE
135 DLILSGRIME AKETFENILD HSNHLMLFSE EINFNDCREM LGNFPQAITH LGVIRAAIKL
136 DEALRGK
137 //
138 ID Q41US7_FERAC Unreviewed; 270 AA.
139 AC Q41US7;
140 DT 27-SEP-2005, integrated into UniProtKB/TrEMBL.
141 DT 27-SEP-2005, sequence version 1.
142 DT 31-OCT-2006, entry version 6.
143 DE Potassium channel protein.
144 GN ORFNames=FaciDRAFT_1443;
145 OS Ferroplasma acidarmanus Fer1.
146 OC Archaea; Euryarchaeota; Thermoplasmata; Thermoplasmatales;
147 OC Ferroplasmaceae; Ferroplasma.
148 OX NCBI_TaxID=333146;
149 RN [1]
150 RP NUCLEOTIDE SEQUENCE.
151 RC STRAIN=Fer1;
152 RG US DOE Joint Genome Institute (JGI-PGF);
153 RA Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina T.,
154 RA Hammon N., Israni S., Pitluck S., Richardson P.;
155 RT "Sequencing of the draft genome and assembly of Ferroplasma
156 RT acidarmanus fer1.";
157 RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
158 RN [2]
159 RP NUCLEOTIDE SEQUENCE.
160 RC STRAIN=Fer1;
161 RG US DOE Joint Genome Institute (JGI-ORNL);
162 RA Larimer F., Land M.;
163 RT "Annotation of the draft genome assembly of Ferroplasma acidarmanus
164 RT fer1.";
165 RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
166 RN [3]
167 RP NUCLEOTIDE SEQUENCE.
168 RC STRAIN=Fer1;
169 RG US DOE Joint Genome Institute (JGI-PGF);
170 RA Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina T.,
171 RA Hammon N., Israni S., Pitluck S., Richardson P.;
172 RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
173 CC -!- CAUTION: The sequence shown here is derived from an
174 CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
175 CC preliminary data.
176 CC -----------------------------------------------------------------------
177 CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
178 CC Distributed under the Creative Commons Attribution-NoDerivs License
179 CC -----------------------------------------------------------------------
180 DR EMBL; AABC04000002; EAM94333.1; -; Genomic_DNA.
181 DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
182 DR GO; GO:0006813; P:potassium ion transport; IEA:InterPro.
183 DR InterPro; IPR013099; Ion_trans_2.
184 DR InterPro; IPR003148; TrkA_N.
185 DR Pfam; PF07885; Ion_trans_2; 1.
186 DR Pfam; PF02254; TrkA_N; 1.
187 DR PROSITE; PS51201; RCK_N; 1.
188 KW Ionic channel.
189 SQ SEQUENCE 270 AA; 30497 MW; 528C4EA75C41DF75 CRC64;
190 MQTITTVGYG DTPVYGLAGR ANGMLIMVIG IGSLGYLMAG LTSMLIDIRL SSKLGERMAA
191 EKKHIVLCNY NESTKKVLDK IKYDGIDIVI LNENEVKGDN EYTYIKGSFL RENDLIRAGI
192 KKASSVIIFS RSEDKEQMAM DAESILSAMI IRKLNPEIRI IGEILNPDSR EHASSFMDDI
193 IIKGDVSSML IYSSIMIPGI PEFINDLLMS NSISEEDIDK KYASNTYREF ISNMEKENRI
194 VLAFRKQDKI YLRENSDKKI DVDSYIFIKN
195 //