ID A0A2U1VQ36_9PROT Unreviewed; 965 AA.
AC A0A2U1VQ36;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:PWC36949.1};
GN ORFNames=TSO221_28560 {ECO:0000313|EMBL:PWC36949.1};
OS Azospirillum sp. TSO22-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=716789 {ECO:0000313|EMBL:PWC36949.1, ECO:0000313|Proteomes:UP000245126};
RN [1] {ECO:0000313|EMBL:PWC36949.1, ECO:0000313|Proteomes:UP000245126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSO22-1 {ECO:0000313|EMBL:PWC36949.1,
RC ECO:0000313|Proteomes:UP000245126};
RA Jang J., Ishii S.;
RT "Comparative genome analysis of Azospirillum sp. strains.";
RL Submitted (JUL-2015) 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}.
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:PWC36949.1}.
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DR EMBL; LGQZ01000133; PWC36949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1VQ36; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000245126; 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 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:UP000245126};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 68..124
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 965 AA; 106711 MW; 153371FB1EAC3D9C CRC64;
MLTKRSSGTA PRGHLARSLT AGTGKGVSRR GFLHGSGLAA GGMAALSALP AAMIRRAEAA
GPIPGAETVT RKNICTHCSV GCTVIAEIQN GVWTGQEPGW ESPISQGTHC AKGASVRELT
TGERRVKYPL KLVDGEWKRI SWDVAIEEIG NKLLEIRRTS GPDSVFWLGS AKFSNEGSYL
FRKLAAFWGT NNVDHQARIC HSTTVAGVAN TWGYGAMTNS YNDIQNSKCL VLIGGNPAEA
HPVSMQHMLR GKERNRAPFI VIDPRFTRTA AHATEYVRIR PGTDIPVVWG ILWHVFEQGW
EDKEYIRQRV YGMDQVRAEV KKWTPQEVER VSGVPGEQLK RVAEAMAKNR PSTLIWCMGA
TQKSVGTANV RAFSILQLAL GNIGIEGGGA NIYRGHCNVQ GATDFGLDVS TLPSYYGLAE
GAWKHFCRVW EVDYEWMKSR FASKALMEAK GIPTTRWFDA VLAKKEDVEQ PDTLKAMLCF
GHGGNTVTRM PEMVKGLEKL ELLVIADPHP TTFASISGRK NGSYILPGCT QFETDGSRTC
SNRSMQWGEK LVEPIFESKD DYTIIYLLAK KLGFADEMFK HITVEGTRPV PEDILREINR
SCLSTGYTGQ SPERLKLHMK HQADFDKITM RAESGPCKGE YYGLPWPCWG HPELKHPGSA
ILYDTSKHVM EGGGVFRARF GVEREGVSLL AEGSYSKGSE IQDGYPEFTM AVLRKLGWDK
DLTAEEMRVI QAIGGDKIDE VSWQTDLSMG IIRVALKHGC SPHGNAKARA AAWNLPDPVP
VHREPIYTPR KDLVSQYPAI NDRRDFRLPQ LAKSVQAGAV DKDVAGKFPF VLTSGRLVEY
EGGGEETRSN RWLAELQQSM FAEINSKDAE RLGIRNDAWV WVYGPENNAK VKVRALVTNR
VGPGTVFMPF HFSGYWQGES RRAAYPPGTD PIVLGESANT VTTYGYDPVT FMQEAKVTLC
RVEPA
//
