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Database: UniProt
Entry: A0A0W0VB12_9GAMM
LinkDB: A0A0W0VB12_9GAMM
Original site: A0A0W0VB12_9GAMM 
ID   A0A0W0VB12_9GAMM        Unreviewed;       402 AA.
AC   A0A0W0VB12;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Threonine(-3-)dehydrogenase {ECO:0000313|EMBL:KTD17301.1};
GN   ORFNames=Ljor_1607 {ECO:0000313|EMBL:KTD17301.1};
OS   Legionella jordanis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=456 {ECO:0000313|EMBL:KTD17301.1, ECO:0000313|Proteomes:UP000055035};
RN   [1] {ECO:0000313|EMBL:KTD17301.1, ECO:0000313|Proteomes:UP000055035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL-540 {ECO:0000313|EMBL:KTD17301.1,
RC   ECO:0000313|Proteomes:UP000055035};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KTD17301.1}.
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DR   EMBL; LNYJ01000011; KTD17301.1; -; Genomic_DNA.
DR   RefSeq; WP_058471069.1; NZ_RDQQ01000018.1.
DR   AlphaFoldDB; A0A0W0VB12; -.
DR   STRING; 456.Ljor_1607; -.
DR   PATRIC; fig|456.5.peg.1716; -.
DR   OrthoDB; 9773078at2; -.
DR   Proteomes; UP000055035; Unassembled WGS sequence.
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; 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:SF7; ALCOHOL DEHYDROGENASE (ZN-DEPENDENT)-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:UP000055035};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          27..147
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          189..258
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   402 AA;  43204 MW;  CD85C40A829E796F CRC64;
     MRALVYHGIG NIRFEEVSKP TIQDDYDAIV KITTSAICGT DLHFIRGTVG PMKKGTILGH
     EAVGVVEEVG SAVKNFREGE RVIIPSTVAC GYCEMCHLGF YSQCNQANPN GPEAGTAFFG
     GPEMTGPLQG CQAEYVRVPF ANHNLVKLPD RVRDDQAILL SDIFPTAYFS VDIAGAKTGD
     VAVVLGCGPV GQFAIASCKL RGVSRIIAID AIPSRLDLAK KQGAECINFN EEEPLAMVKE
     LTNGLGANVV IDAVGIDAYA PEKGPAAKKA AKQKGEFEEE LSNLVPAVRN DGPNWIPGNA
     PSYTLREAVD LVAKCGTVSI IGVYPQNFKV YPIGKAMNKN LKLVMGNCPH RAYIPKLLAM
     VEAGLIDPTG ILTQQEPLTD ILEAYKQFDL RKDGWIKVAL TV
//
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