GenomeNet

Database: UniProt
Entry: A0A2U1VDB0_9PROT
LinkDB: A0A2U1VDB0_9PROT
Original site: A0A2U1VDB0_9PROT 
ID   A0A2U1VDB0_9PROT        Unreviewed;       563 AA.
AC   A0A2U1VDB0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:PWC32087.1};
DE   Flags: Fragment;
GN   ORFNames=TSO221_31535 {ECO:0000313|EMBL:PWC32087.1};
OS   Azospirillum sp. TSO22-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=716789 {ECO:0000313|EMBL:PWC32087.1, ECO:0000313|Proteomes:UP000245126};
RN   [1] {ECO:0000313|EMBL:PWC32087.1, ECO:0000313|Proteomes:UP000245126}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSO22-1 {ECO:0000313|EMBL:PWC32087.1,
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   -!- 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:PWC32087.1}.
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; LGQZ01000166; PWC32087.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1VDB0; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000245126; Unassembled WGS sequence.
DR   GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
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:InterPro.
DR   GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR   CDD; cd02790; MopB_CT_Formate-Dh_H; 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; IPR041925; CT_Formate-Dh_H.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245126}.
FT   DOMAIN          8..363
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          450..554
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PWC32087.1"
SQ   SEQUENCE   563 AA;  61499 MW;  C9872D23462FE5F9 CRC64;
     LVRTGFGTNN VDHCTRLCHA SSVAALIEGI GSGAVTAPFM AAEDAEVIVV IGSNPTENHP
     VAATFFKNAV KKGAKLVIMD PRGTAMRRHA SHMMQFKPGR DVPMLNAMLN VIISEGLYDA
     TYVAEHTQDF EELKAHVAAL TPEAMAPVCG IDAQTLRDVA RLYATSKASI IFWGMGVSQH
     THGTDNVRCL IALSLVTGHI GRPGTGLHPL RGQNNVQGAS DAGLIPMMYP DYRPVDDPKV
     HAFYEDFWQT KLETKRGLTV VETMDAIHAG KVRGMYVMGE NPAMSDPDVQ HAREALADLE
     HLVVQDLFLT ETAKYADVVL PASAWPEKNG TVTNTNRQVQ LGRQALPPPG DARQDLWILR
     ELARGLGLDW TYEHPRDVFI EMKGAMPSLD NITWDRLERE GSVTYPSLSP DDPGQEIVFG
     DGFPTATGRG RLVPADVIPP AEEPDQEFPM VLTTGRQLEH WHTGSMTRRA QVLDDIEPEA
     VAYMSPADLR RMGAKGGDRV KVTTRRGVIE LKARSDYGVP TGLVFIPFCY AEAAANVLTN
     PKLDPFGKIP EFKFAAARIE PAA
//
DBGET integrated database retrieval system