ID   Q12S79_SHEDO            Unreviewed;       379 AA.
AC   Q12S79;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   SubName: Full=Alanine-glyoxylate aminotransferase {ECO:0000313|EMBL:ABE53697.1};
DE            EC=2.6.1.44 {ECO:0000313|EMBL:ABE53697.1};
GN   OrderedLocusNames=Sden_0404 {ECO:0000313|EMBL:ABE53697.1};
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161 {ECO:0000313|EMBL:ABE53697.1, ECO:0000313|Proteomes:UP000001982};
RN   [1] {ECO:0000313|EMBL:ABE53697.1, ECO:0000313|Proteomes:UP000001982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS217 / ATCC BAA-1090 / DSM 15013
RC   {ECO:0000313|Proteomes:UP000001982};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR000524-50, ECO:0000256|RuleBase:RU004504};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009236,
CC       ECO:0000256|RuleBase:RU004075}.
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DR   EMBL; CP000302; ABE53697.1; -; Genomic_DNA.
DR   RefSeq; WP_011494863.1; NC_007954.1.
DR   AlphaFoldDB; Q12S79; -.
DR   STRING; 318161.Sden_0404; -.
DR   KEGG; sdn:Sden_0404; -.
DR   eggNOG; COG0075; Bacteria.
DR   HOGENOM; CLU_027686_0_0_6; -.
DR   OrthoDB; 9766472at2; -.
DR   Proteomes; UP000001982; Chromosome.
DR   GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
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; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR   PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000524; SPT; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ABE53697.1};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000524-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001982};
KW   Transferase {ECO:0000313|EMBL:ABE53697.1}.
FT   DOMAIN          37..344
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         354
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT   MOD_RES         202
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ   SEQUENCE   379 AA;  40991 MW;  9F3CE356F27102A9 CRC64;
     MISAPTVNSF TPPRRTLMGP GPSDVYPEVL AAQARPTIGH LDPLFVGMMD ELKSLIQYAF
     QTKNEMTLAI SAPGSAGMEA CFVNLVEPGE KVIVCRNGVF GERMRQNVER VGALAVVVDN
     EWGEPVCPKA VEAALKANPD AKFLAFVHAE TSTGALSDAK TLCRLAQEHD CLSIVDAVTS
     LGGVELLVDE WGIDAIYSGS QKCLSCVPGL SPVSFSPKAV AKLMSRKTPV QSWFLDQSLV
     MGYWGNKDSG LKRSYHHTAP VNALYALHEA FRLLALEGLE NAWARHKKMH LVLAAGLEQL
     GLKFVVAAEH RLPQLNAVYL PQGVDDALVR TQLLEEYNLE IGAGLGALAG KAWRIGLMGF
     GARRENVALC LKALEEVMN
//