ID A0A013VC41_9SPHN Unreviewed; 756 AA.
AC A0A013VC41;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:EXS68914.1};
GN ORFNames=BF95_00990 {ECO:0000313|EMBL:EXS68914.1};
OS Sphingobium sp. Ant17.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1461752 {ECO:0000313|EMBL:EXS68914.1, ECO:0000313|Proteomes:UP000021537};
RN [1] {ECO:0000313|EMBL:EXS68914.1, ECO:0000313|Proteomes:UP000021537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ant17 {ECO:0000313|EMBL:EXS68914.1,
RC ECO:0000313|Proteomes:UP000021537};
RA Adriaenssens E.M., Cowan D.A.;
RT "Draft genome sequence of the aromatic hydrocarbon-degrading bacterium
RT Sphingobium sp. strain Ant17 isolated from Antarctic soil.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXS68914.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JEMV01000053; EXS68914.1; -; Genomic_DNA.
DR RefSeq; WP_051520120.1; NZ_JEMV01000053.1.
DR AlphaFoldDB; A0A013VC41; -.
DR STRING; 1461752.BF95_00990; -.
DR PATRIC; fig|1461752.3.peg.4171; -.
DR OrthoDB; 5287431at2; -.
DR Proteomes; UP000021537; Unassembled WGS sequence.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR CDD; cd02787; MopB_CT_ydeP; 1.
DR CDD; cd02767; MopB_ydeP; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037951; MopB_CT_YdeP.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR010046; Mopterin_OxRdtse_a_bac.
DR InterPro; IPR041953; YdeP_MopB.
DR NCBIfam; TIGR01701; Fdhalpha-like; 1.
DR PANTHER; PTHR43105:SF4; PROTEIN YDEP; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF000144; CbbBc; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 110..481
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 641..748
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 756 AA; 83110 MW; D89CA4AA2C05F663 CRC64;
MANPPKTVEY DSATGGWGSL RGMGETALGE RSTPGAFETL RSQNKTGGFM CTSCAWGKPK
HPHAFEFCEN GAKATLWELT THRCTPDFFA KHSVTELRGW SDHDLEHEGR LTHPLRYDAA
SDHYVPCSWD EAFSAIGAEL QAIDPKSAIF YASGRASLET SYVYALFARL YGHNNLPDSS
NMCHETTSVT LNALIGSPVG TCILDDFEQC DAIFFFGQNT GTNSPRFLHP LQKAVERGCK
VVTFNPIREK GLIEFINPQR PTQMLTGNGT PISCQYLQVR AGGDIAAIMG LCKYVFAEDE
RRGGTLIDQA FIDEHCLGFD AFRAKADATT WDRIEQESGL SRADIEEAGR VYVEAERVIG
VYGMGLTQHV HGFENIAMLV NLLLMRGHIG RTGAGICPVR GHSNVQGQRT VGISEKPELV
PLDTFAAQFD FDPPRDTGMT TVEVCEGVLD ETVQAFIGLG GNFLRAIPDQ ARIESAWERM
RLTVQIATKL NRGHLFNGKT AYLLPCLGRS EEDMQAGGPQ TVTIEDSFSH IHASIGHRTP
ASEHLKSEMA IVAGIAKATL MPNPKVRWDA WTGDYSLVRD LIAETYHEEF HDMNARIFEP
GGFYRGNGAR ERIWKTKTGK AQFTAPAMLA ATDVADVDGR YRLVTVRSND QFNTTIYGYS
DRLRGIEGKR DVILINPADM AAAGLSEGQR VALVGDAGDG HVRRIDNLEI VPFDLPDGTI
VGYYPELNPL IALHHHDRNS KTPASKAVPV RIEAAP
//
