ID   C3LNS8_VIBCM            Unreviewed;       404 AA.
AC   C3LNS8;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=VCM66_1901 {ECO:0000313|EMBL:ACP06204.1};
OS   Vibrio cholerae serotype O1 (strain M66-2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=579112 {ECO:0000313|EMBL:ACP06204.1, ECO:0000313|Proteomes:UP000001217};
RN   [1] {ECO:0000313|EMBL:ACP06204.1, ECO:0000313|Proteomes:UP000001217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M66-2 {ECO:0000313|EMBL:ACP06204.1,
RC   ECO:0000313|Proteomes:UP000001217};
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR   EMBL; CP001233; ACP06204.1; -; Genomic_DNA.
DR   RefSeq; WP_001179458.1; NC_012578.1.
DR   AlphaFoldDB; C3LNS8; -.
DR   GeneID; 69719395; -.
DR   KEGG; vcm:VCM66_1901; -.
DR   HOGENOM; CLU_017584_4_2_6; -.
DR   Proteomes; UP000001217; Chromosome I.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43488; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR   PANTHER; PTHR43488:SF2; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ACP06204.1};
KW   Transferase {ECO:0000313|EMBL:ACP06204.1}.
FT   DOMAIN          35..394
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   404 AA;  45219 MW;  A4D8BD4720B2C532 CRC64;
     MQNIGMSSKL DNVCYDIRGP VLKHAKRMEE EGHKILKLNI GNPAPFGFDA PDEILVDVIR
     NLPTSQGYCD SKGIYSARKA VVQYYQKKGI RSLDVEDVYI GNGASELIVM AMQALLNNGD
     EMLVPAPDYP LWTAAVALSG GKAVHYICDE EADWYPDLDD IRSKITPKTR GIVLINPNNP
     TGAVYSRDFL LEIIEIARKH KLMIFADEIY DKVLYDGAVH TSIATLADDV LVVTFNGLSK
     AYRVCGFRGG WMFLTGPKQQ AQGYIAGLDM LASMRLCANV PMQHAIQTAL GGYQSINELI
     LPGGRLLEQR DRAWELINQI PGISCVKPKG AMYLFPKIDT KMYPIKDDQK MVLDFLVQEK
     VLLVQGSGFN WPKPDHFRIV TLPHVEDLEI AISRFERFIT TYSQ
//