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Database: UniProt
Entry: A0A077LRA3_9PSED
LinkDB: A0A077LRA3_9PSED
Original site: A0A077LRA3_9PSED 
ID   A0A077LRA3_9PSED        Unreviewed;       400 AA.
AC   A0A077LRA3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Formaldehyde dehydrogenase {ECO:0000313|EMBL:BAP45703.1};
GN   ORFNames=PSCI_5001 {ECO:0000313|EMBL:BAP45703.1};
OS   Pseudomonas sp. StFLB209.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1028989 {ECO:0000313|EMBL:BAP45703.1, ECO:0000313|Proteomes:UP000031652};
RN   [1] {ECO:0000313|EMBL:BAP45703.1, ECO:0000313|Proteomes:UP000031652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StFLB209 {ECO:0000313|EMBL:BAP45703.1,
RC   ECO:0000313|Proteomes:UP000031652};
RX   PubMed=25323715; DOI=10.1128/genomeA.01037-14;
RA   Morohoshi T., Kato T., Someya N., Ikeda T.;
RT   "Complete Genome Sequence of N-Acylhomoserine Lactone-Producing Pseudomonas
RT   sp. Strain StFLB209, Isolated from Potato Phyllosphere.";
RL   Genome Announc. 2:e01037-e01014(2014).
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; AP014637; BAP45703.1; -; Genomic_DNA.
DR   RefSeq; WP_045492230.1; NZ_AP014637.1.
DR   AlphaFoldDB; A0A077LRA3; -.
DR   STRING; 1028989.PSCI_5001; -.
DR   KEGG; pses:PSCI_5001; -.
DR   HOGENOM; CLU_026673_11_3_6; -.
DR   OrthoDB; 9773078at2; -.
DR   Proteomes; UP000031652; Chromosome.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08282; PFDH_like; 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; IPR014184; HCHO_DH_non_GSH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR02819; fdhA_non_GSH; 1.
DR   PANTHER; PTHR42813:SF3; GLUTATHIONE-INDEPENDENT FORMALDEHYDE DEHYDROGENASE; 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:UP000031652};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          36..146
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          198..265
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   400 AA;  42038 MW;  46E2A102B483A383 CRC64;
     MSTGNRGVVY LGAGKVEVQN IDYPKMQDPR GKKIEHGVIL KVVATNICGS DQHMVRGRTT
     AQIGLVLGHE ITGEVIEKGS DVESLKIGDL VSVPFNVACG RCRSCKEMHT GVCLTVNPAR
     PGGAYGYVDM GDWTGGQAEY VLVPYADFNL LKLPNRDKAM EKIRDLTCLS DILPTGFHGA
     VTAGVGPGST VYVAGAGPVG LAAAASARLL GAAVVIVGDL NPARLAHAKA QGFEIADLST
     DTPLHEQIAA LLGEPEVDCA IDAVGFEARG HGHEGAKHEA PATVLNSLMQ VTRVAGKIGI
     PGLYVTEDPG AVDAAAKNGA LSIRFGLGWA KSHSFHTGQT PTMKYNRQLM QAIMWDRLNI
     AEIVGVQVIS LDQAPAGYGE FDAGVPKKFV IDPHKTFSAA
//
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