ID A0A2P5GM52_9ENTR Unreviewed; 715 AA.
AC A0A2P5GM52;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:POP46561.1};
GN ORFNames=CHU32_17750 {ECO:0000313|EMBL:POP46561.1};
OS Superficieibacter electus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Superficieibacter.
OX NCBI_TaxID=2022662 {ECO:0000313|EMBL:POP46561.1, ECO:0000313|Proteomes:UP000247005};
RN [1] {ECO:0000313|EMBL:POP46561.1, ECO:0000313|Proteomes:UP000247005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BP-1 {ECO:0000313|EMBL:POP46561.1,
RC ECO:0000313|Proteomes:UP000247005};
RA Potter R.F., D'Souza A.W.;
RT "Superficieibacter electus gen. nov., sp. nov., an extended-spectrum beta-
RT lactamase possessing member of the Enterobacteriaceae family, isolated from
RT intensive care unit surfaces.";
RL Submitted (JAN-2018) 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 -!- 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:POP46561.1}.
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DR EMBL; PQGD01000014; POP46561.1; -; Genomic_DNA.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000247005; Unassembled WGS sequence.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; 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:0045333; P:cellular respiration; IEA:UniProt.
DR GO; GO:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd02790; MopB_CT_Formate-Dh_H; 1.
DR CDD; cd02753; MopB_Formate-Dh-H; 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 Gene3D; 1.20.5.460; Single helix bin; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041925; CT_Formate-Dh_H.
DR InterPro; IPR041924; Formate_Dh-H_N.
DR InterPro; IPR006478; Formate_DH_asu.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF000144; CbbBc; 2.
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; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 4: Predicted;
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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Selenium {ECO:0000313|EMBL:POP46561.1};
KW Selenocysteine {ECO:0000313|EMBL:POP46561.1}.
FT DOMAIN 1..56
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT NON_STD 140
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:POP46561.1"
SQ SEQUENCE 715 AA; 79160 MW; D867EAC21EB99244 CRC64;
MKKVVTVCPY CASGCKINLV VDNGKIVRAE AAQGKTNQGT LCLKGYYGWD FINDTQILTP
RLKTPMIRRQ RGGKLEAVSW DEALNYVADR LSAIKAKYGP DAIQTTGSSR GTGNETNYVM
QKFARAAIGT NNVDCCARVU HGPSVAGLHQ SVGNGAMSNA INEIDNTDLV FVFGYNPADS
HPIVANHVIN AKRNGAKIIV CDPRKIETAR IADMHIALKN GSNIALLNAI GHVIIEEKLY
DQAFVASRTE GFEEYRKIVE GYTPESVEDI TGISADEIRK CARMYAGAKS AAILWGMGVT
QFYQGVETVR SLTSLAMLTG NLGKPHAGVN PVRGQNNVQG ACDMGALPDT YPGYQYVKFP
ENREKFAKAW GVESLPAHTG YRISELPHRA AHGEVRAAYI MGEDPLQTDA ELSAVRKGFE
DLELVIVQDI FMTKTAAAAD VILPSTSWGE HEGVFSAADR GFQRFFKAVE PKWDLKTDWQ
IISEIATRMG YPMHYNNTQE IWDELRNLCP DFYGATYEKM GELGYIQWPC RDTSDADQGT
SYLFKEKFDT PNGLAQFFTC DWVAPIDKLT DEYPMVLSTV REVGHYSCRS MTGNCAALAA
LADEPGYAQI NTADAARLGI EDEALVWVNS RKGRIITRAQ VSDRPNKGAI YMTYQWWIGA
CNELVTENLS PITKTPEYKY CAVNVERITD QRAAEQYVID EYNKLKSSLR ESAMG
//
