ID Q8P970_XANCP Unreviewed; 389 AA.
AC Q8P970;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 24-JAN-2024, entry version 124.
DE SubName: Full=Glutathione-dependent formaldehyde dehydrogenase {ECO:0000313|EMBL:AAM41285.1};
GN Name=fdh {ECO:0000313|EMBL:AAM41285.1};
GN OrderedLocusNames=XCC1996 {ECO:0000313|EMBL:AAM41285.1};
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485 {ECO:0000313|EMBL:AAM41285.1, ECO:0000313|Proteomes:UP000001010};
RN [1] {ECO:0000313|EMBL:AAM41285.1, ECO:0000313|Proteomes:UP000001010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25
RC {ECO:0000313|Proteomes:UP000001010};
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F.Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P.Jr., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A.Jr., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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DR EMBL; AE008922; AAM41285.1; -; Genomic_DNA.
DR RefSeq; NP_637361.1; NC_003902.1.
DR RefSeq; WP_011037159.1; NC_003902.1.
DR AlphaFoldDB; Q8P970; -.
DR STRING; 190485.XCC1996; -.
DR EnsemblBacteria; AAM41285; AAM41285; XCC1996.
DR KEGG; xcc:XCC1996; -.
DR PATRIC; fig|190485.4.peg.2132; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_3_6; -.
DR OMA; AMYGHRD; -.
DR OrthoDB; 9773078at2; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08283; FDH_like_1; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001010};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 26..149
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 196..266
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 389 AA; 42193 MW; 6BD8F3056AD3C3A2 CRC64;
MRALCWNGVN DLRVETVPDP VLVNPRDVIL KVGLSTTCGS DLHFIDGYLP TMREGDVIGH
EFMGTVVEVG PAVKNVRVGQ RVVVPSFISC GGCWHCERKE YSLCDNTNPH WEMQESLLGH
PTAGIYGYTH AFGGYAGSHA TYIRVPHADV GCFEVPDEVS DEDALFLSDA GPTGFMGADF
CNIQPGDTVA VWGCGGVGLM AQQSARILGA ERVIAIDRLP ERLAMARDVL GVEVIDYSTV
DSVVDVLREM TGGRGPDACI DAVGMEAHGT GMGHAYDRVK QALHLHTDRG QALREAILAC
RKGGILSVLG VYGLMDKFPL GAVMNKGLTM RTAQQHGQLY VPRLLDLARA GRLKSSFLMT
HKMPLEEAAR GYEMFKHKHE GCVRAAFVP
//