ID A0A1U7DKK5_9RHOB Unreviewed; 1088 AA.
AC A0A1U7DKK5; A0A2M9DCG3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:APX90423.1, ECO:0000313|EMBL:PJJ85482.1};
GN ORFNames=BV394_12360 {ECO:0000313|EMBL:APX90423.1}, CLV77_2352
GN {ECO:0000313|EMBL:PJJ85482.1};
OS Brevirhabdus pacifica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Brevirhabdus.
OX NCBI_TaxID=1267768 {ECO:0000313|EMBL:APX90423.1, ECO:0000313|Proteomes:UP000187266};
RN [1] {ECO:0000313|EMBL:APX90423.1, ECO:0000313|Proteomes:UP000187266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY6-4 {ECO:0000313|EMBL:APX90423.1,
RC ECO:0000313|Proteomes:UP000187266};
RA Wang X.;
RT "Genomic analysis of Xuhuaishuia manganoxidans DY6-4.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PJJ85482.1, ECO:0000313|Proteomes:UP000229573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27767 {ECO:0000313|EMBL:PJJ85482.1,
RC ECO:0000313|Proteomes:UP000229573};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) 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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP019124; APX90423.1; -; Genomic_DNA.
DR EMBL; PGFI01000012; PJJ85482.1; -; Genomic_DNA.
DR RefSeq; WP_076980441.1; NZ_PGFI01000012.1.
DR AlphaFoldDB; A0A1U7DKK5; -.
DR STRING; 1267768.BV394_12360; -.
DR Proteomes; UP000187266; Chromosome.
DR Proteomes; UP000229573; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS51318; TAT; 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 Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000187266};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 72..128
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1088 AA; 120989 MW; 19AC528184D2EAE3 CRC64;
MLKRKTFDRP GQSPSAPRPG RAAPLGAAEA SAPSRRDFLR NSGLMGLALG AGWSAGTVQR
AEASTPYTSG EVTRHKTICH FCSVGCSVWA EVQQGVWIGQ EPVFESPVNQ GTHCAKGAAM
REIAISERRL KYPMKKEGGV WKRISWDQAM QEIAEKQLAI REKYGPDSSY WLGSAKFSNE
QSYLFRKFVA FWGTNNIDHQ ARICHSTTVA GVANTFGYGA MTNTFNDIRN SRSIIILGGN
PAEAHPVSML HVLAGKENGA PLIVVDPRFT RTAAHADEYV RIRPGADVGF INGLIREILA
NGWEDREYLR QRVFGLDELR AEVEKWTPEE VERVSGIPAD QTRRVARTLA ENRPGTLIWC
MGLTQSHIGN NKTRAASILQ LVLGNIGKSG GGTNIFRGHD NVQGATDMGV SCDTLPAYYG
LSEGAWKHWA RVWGVDYDWV KGRFGSKELM EKAGMPVSRW LDGVLEDPAN LEQPNPVKAM
TFWGHAANSL TRGPEQRAAL DTVELLTIID PHPTQVAIMT DKTDGVYLLP AASTAESHGT
VTNSNRSVQM RDQVVDPIFE SKTDYEIVRL FAEAFGFADK LFQGIRIVDG VPDAYDLLRE
INRGCWTIGY TGQSPERLRL HMDHQDKFDS VSLLGKEEPV KGEYYCLPWP AWGKDTHGHP
GTPLLYDTSK SVREGGLPFR ARWGVEHEGR NLLAEDSFTK GSEIRDGYPE GTIGMLQALG
WAGELTDREM LIAVAIAADR FSLDMLEMPD AEVRDAMDRL EEFARQNRLD RKGEALATDE
GSWQGGPFEA NTGGNGDGTK KPGDKPAEKK AEKKNKEKAD SNAPTDRASV RRRFPDYPDN
AITAISAYLA DNPQDDPKPD APLRDKIMRV NWKTDLSGGV QRVMLAHNLA PYGNGKARMV
VWNFPDPVPV HREPLYTVRR DLLPEYKTLE DRRMWRLPVL YESIQEQDYS QEFPMILTSG
RLVEFEGGGD ETRSNKWLAE FQQQMFVEIN PADAGAAGIE NKAFCWVRTP VGNLRVQAMV
TRRVDPGVAF MPFHFAGMWM GEDLSHRYPV GTVPYVIGEA SNTAQTYGYD SVTQMQETKA
TICRIEPA
//
