ID K6Y9H0_9ALTE Unreviewed; 374 AA.
AC K6Y9H0;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Alanine-glyoxylate transaminase {ECO:0000313|EMBL:GAC14822.1};
GN ORFNames=GLIP_2194 {ECO:0000313|EMBL:GAC14822.1};
OS Aliiglaciecola lipolytica E3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Aliiglaciecola.
OX NCBI_TaxID=1127673 {ECO:0000313|EMBL:GAC14822.1, ECO:0000313|Proteomes:UP000006334};
RN [1] {ECO:0000313|EMBL:GAC14822.1, ECO:0000313|Proteomes:UP000006334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:GAC14822.1,
RC ECO:0000313|Proteomes:UP000006334};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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}.
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:GAC14822.1}.
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DR EMBL; BAEN01000041; GAC14822.1; -; Genomic_DNA.
DR RefSeq; WP_008844638.1; NZ_BAEN01000041.1.
DR AlphaFoldDB; K6Y9H0; -.
DR STRING; 1127673.GLIP_2194; -.
DR eggNOG; COG0075; Bacteria.
DR OrthoDB; 9766472at2; -.
DR Proteomes; UP000006334; Unassembled WGS sequence.
DR GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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; IPR002034; AIPM/Hcit_synth_CS.
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.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
PE 3: Inferred from homology;
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:UP000006334}.
FT DOMAIN 35..339
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 200
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 374 AA; 41044 MW; BB0EEC64F3C5587A CRC64;
MNSFATSFIP TIRTLMGPGP SDVDPRILTA LSRPTIGHLD PQFIQLMDEI KSLLQYAFQT
KNQLTMPVSA PGSAGMEACF ANLVEPGDKV IVCQNGVFGG RMKENVLRCG GIPIMVEDQW
GKPTDLNKLE HTLNNHSDAK IVAFVHAETS TGVKNDAQAI CHLAKKFNCL TLVDAVTSLG
GCELSVDEWQ IDAIYSGTQK CLSCVPGLSP VSFSQLAIDA ITSRKTPVQS WFLDMELVMG
YWGKGAKRAY HHTAPVNSLY ALHEALIILQ NEGLETAWQR HQQMHVKLRE GLQALGLEFV
VEEKYRLPQL NMVRIPEGID DAQVRQTLLS EFNLEIGAGL GELAGKVWRI GLMGYGCNSK
NVNYCISAIK SVLS
//
