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Database: UniProt
Entry: S3NCA6_9GAMM
LinkDB: S3NCA6_9GAMM
Original site: S3NCA6_9GAMM 
ID   S3NCA6_9GAMM            Unreviewed;       411 AA.
AC   S3NCA6;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=F945_02335 {ECO:0000313|EMBL:EPF71989.1};
OS   Acinetobacter rudis CIP 110305.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=421052 {ECO:0000313|EMBL:EPF71989.1, ECO:0000313|Proteomes:UP000014568};
RN   [1] {ECO:0000313|EMBL:EPF71989.1, ECO:0000313|Proteomes:UP000014568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 110305 {ECO:0000313|EMBL:EPF71989.1,
RC   ECO:0000313|Proteomes:UP000014568};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter rudis CIP 110305.";
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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:EPF71989.1}.
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DR   EMBL; ATGI01000031; EPF71989.1; -; Genomic_DNA.
DR   RefSeq; WP_016656739.1; NZ_KE340353.1.
DR   AlphaFoldDB; S3NCA6; -.
DR   STRING; 632955.GCA_000829675_01620; -.
DR   PATRIC; fig|421052.3.peg.2279; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_6; -.
DR   OrthoDB; 9803354at2; -.
DR   Proteomes; UP000014568; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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   PRINTS; PR00753; ACCSYNTHASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000014568}.
FT   DOMAIN          42..403
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   411 AA;  46004 MW;  0AB9763DB9526176 CRC64;
     MSVLGYTTPR EIKKSSKLEH VCYDIRGPVL RAANEMEEAG HKIIKLNIGN PAPFGFEAPQ
     EIINDVALNL PNAIGYTDSK GIFPARKAVC QYYQQKNIHD LNVKDVYIGN GVSELIVMAM
     QGLLDDGDEM LVPMPDYPLW TAAINLSGGT AIHYKCDEEN SWYPDIADME AKITANTRGI
     VIINPNNPTG SVYPRHVLEQ IVALAKKHDL LLFADEIYDR IIYDGIEHVS VAELAGDHLC
     ITFNGLSKSH RIAGYRSGWM AITGDKSRAS DYIEGLDMLA SMRLCANHQA QYAIQTALGG
     YQSINDLIRP GGRLYEQRNI AWEMLNEIPG VSCVKPEGAM YCFPQLDPKI YPIEDDEKLM
     LDFLKAEKVL LVQGTGFNWP TPDHFRLVFL PAENELREAI TRLGRFLAKM R
//
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