ID Q9V045_PYRAB Unreviewed; 288 AA.
AC Q9V045;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE SubName: Full=Cytochrome-c3 hydrogenase subunit gamma {ECO:0000313|EMBL:CCE70358.1};
DE SubName: Full=Sulfhydrogenase II, gamma chain {ECO:0000313|EMBL:CAB49861.1};
GN Name=hydG-2 {ECO:0000313|EMBL:CAB49861.1};
GN ORFNames=PAB0639 {ECO:0000313|EMBL:CAB49861.1};
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844 {ECO:0000313|EMBL:CAB49861.1, ECO:0000313|Proteomes:UP000000810};
RN [1] {ECO:0000313|EMBL:CAB49861.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Orsay {ECO:0000313|EMBL:CAB49861.1};
RA Genoscope;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAB49861.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Orsay {ECO:0000313|EMBL:CAB49861.1};
RX PubMed=10736225; DOI=10.1006/jmbi.2000.3593;
RA Gaspin C., Cavaille J., Erauso G.;
RT "Archaeal homologs of eukaryotic methylation guide small nucleolar RNAs:
RT lessons from the Pyrococcus genomes.";
RL J. Mol. Biol. 297:895-906(2000).
RN [3] {ECO:0000313|EMBL:CAB49861.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Orsay {ECO:0000313|EMBL:CAB49861.1};
RX PubMed=11381026; DOI=10.1101/gr.GR1653R;
RA Lecompte O., Ripp R., Puzos-Barbe V., Duprat S., Heilig R., Dietrich J.,
RA Thierry J.C., Poch O.;
RT "Genome evolution at the genus level: comparison of three complete genomes
RT of hyperthermophilic archaea.";
RL Genome Res. 11:981-993(2001).
RN [4] {ECO:0000313|EMBL:CAB49861.1, ECO:0000313|Proteomes:UP000000810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay {ECO:0000313|Proteomes:UP000000810}, and Orsay
RC {ECO:0000313|EMBL:CAB49861.1};
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G., Barbe V., Flament D., Galperin M., Heilig R., Ripp R.,
RA Lecompte O., Prieur D., Poch O., Quellerou J., Thierry J.C.,
RA Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [5] {ECO:0000313|EMBL:CCE70358.1, ECO:0000313|Proteomes:UP000009139}
RP GENOME REANNOTATION.
RC STRAIN=GE5 {ECO:0000313|EMBL:CCE70358.1}, and GE5 / Orsay
RC {ECO:0000313|Proteomes:UP000009139};
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|PIRSR:PIRSR006816-2};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000256|PIRSR:PIRSR006816-2};
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DR EMBL; AJ248286; CAB49861.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70358.1; -; Genomic_DNA.
DR PIR; H75069; H75069.
DR RefSeq; WP_010868070.1; NC_000868.1.
DR AlphaFoldDB; Q9V045; -.
DR STRING; 272844.PAB0639; -.
DR GeneID; 1496302; -.
DR KEGG; pab:PAB0639; -.
DR PATRIC; fig|272844.11.peg.1004; -.
DR eggNOG; arCOG02199; Archaea.
DR HOGENOM; CLU_003827_1_1_2; -.
DR OrthoDB; 35401at2157; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro.
DR CDD; cd06221; sulfite_reductase_like; 1.
DR Gene3D; 2.10.240.10; Dihydroorotate dehydrogenase, electron transfer subunit; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR012165; Cyt_c3_hydrogenase_gsu.
DR InterPro; IPR037117; Dihydroorotate_DH_ele_sf.
DR InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR NCBIfam; NF040830; sulfhyd_ShyC; 1.
DR PANTHER; PTHR43513:SF1; ANAEROBIC SULFITE REDUCTASE SUBUNIT B; 1.
DR PANTHER; PTHR43513; DIHYDROOROTATE DEHYDROGENASE B (NAD(+)), ELECTRON TRANSFER SUBUNIT; 1.
DR Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|PIRSR:PIRSR006816-2};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR006816-2};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR006816-
KW 2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR006816-2};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 4..103
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 250
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 255
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 258
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 270
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
SQ SEQUENCE 288 AA; 32712 MW; 5EEBAC9B24F2370C CRC64;
MNPYQSYDAR IIEVRELTPR EKLFSLKFLD PEVEESFTFK PGQFVIVDIR GHGEFPISLC
SSPTRKPIQL CIRRVGRLTR LIHKFSEGDV IGVRGPYGNG FPLEKMEGAT LILVAGGLGM
APLRSVLWYA IDSGKFEKIY LYYGTKSYED ILFRDEIIYL LKHGEKLNCH VKLAYEVETP
SCVYLEKGFS EKVCKGLVTD LFRGEHFDVE NSYALICGPP VMYKFVIKEL LDKGLSPGRI
YMTLERRMRC GVGKCGHCIV GTSVSIKYIC RDGPVFSYWD ALSTRGLI
//
