ID   F8A5D2_CELGA            Unreviewed;       407 AA.
AC   F8A5D2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=Celgi_0427 {ECO:0000313|EMBL:AEI10949.1};
OS   Cellulomonas gilvus (strain ATCC 13127 / NRRL B-14078) (Cellvibrio gilvus).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=593907 {ECO:0000313|EMBL:AEI10949.1, ECO:0000313|Proteomes:UP000000485};
RN   [1] {ECO:0000313|Proteomes:UP000000485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13127 / NRRL B-14078 {ECO:0000313|Proteomes:UP000000485};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Munk A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA   Woyke T.;
RT   "Complete sequence of Cellvibrio gilvus ATCC 13127.";
RL   Submitted (APR-2011) 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}.
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DR   EMBL; CP002665; AEI10949.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8A5D2; -.
DR   STRING; 593907.Celgi_0427; -.
DR   KEGG; cga:Celgi_0427; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_11; -.
DR   OrthoDB; 9763453at2; -.
DR   Proteomes; UP000000485; Chromosome.
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:AEI10949.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000485};
KW   Transferase {ECO:0000313|EMBL:AEI10949.1}.
FT   DOMAIN          37..398
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   407 AA;  44615 MW;  3B60F880D8EEC5BE CRC64;
     MHLRALDQSA KLRDVLYEIR GATLTEAARL EAEGHAVLKL NTGNPAAFGF EAPHQIVRDV
     IAAIPTAHGY SESQGILSAR RAVVTRYETE PGFPQFDVED VFLGNGVSEL ITMVMQALLD
     EGDEVLIPAP DYPLWTAMTS LSDGKPVHYR CDESTGWQPD LEHLESLITA RTKALVVINP
     NNPTGAVYSR ETLAALADIA RRHSLLLLAD EIYDRILFDD AVHVPLASIA PDLLCLTFNG
     LSKTYRVAGY RSGWMVVTGP REHAKGFLEG IQLLASTRLC ANVPAQHALQ AALGGVQSIE
     ALVAPGGRLH EQRDIAWRGL TSIPGVTCVR PSGALYLFPR LDPEVHQIHD DARLVYDLLV
     SEHILLVQGT GFNWPDPDHL RIVTLPEARV LAEAVERLGN FLASYRQ
//