ID A0A0M4NHZ4_9GAMM Unreviewed; 371 AA.
AC A0A0M4NHZ4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Alanine--glyoxylate aminotransferase {ECO:0000313|EMBL:ALE52026.1};
GN ORFNames=SP60_01480 {ECO:0000313|EMBL:ALE52026.1};
OS Candidatus Thioglobus autotrophicus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Thioglobus.
OX NCBI_TaxID=1705394 {ECO:0000313|EMBL:ALE52026.1, ECO:0000313|Proteomes:UP000058020};
RN [1] {ECO:0000313|EMBL:ALE52026.1, ECO:0000313|Proteomes:UP000058020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EF1 {ECO:0000313|EMBL:ALE52026.1,
RC ECO:0000313|Proteomes:UP000058020};
RX PubMed=26494660;
RA Shah V., Morris R.M.;
RT "Genome Sequence of 'Candidatus Thioglobus autotrophica' Strain EF1, a
RT Chemoautotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL Genome Announc. 3:e01156-15(2015).
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; CP010552; ALE52026.1; -; Genomic_DNA.
DR RefSeq; WP_053950954.1; NZ_CP010552.1.
DR AlphaFoldDB; A0A0M4NHZ4; -.
DR STRING; 1705394.SP60_01480; -.
DR KEGG; tho:SP60_01480; -.
DR PATRIC; fig|1705394.5.peg.297; -.
DR OrthoDB; 9766472at2; -.
DR Proteomes; UP000058020; Chromosome.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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:ALE52026.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000058020};
KW Transferase {ECO:0000313|EMBL:ALE52026.1}.
FT DOMAIN 32..336
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 196
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 371 AA; 40432 MW; 5577A330AFF8691C CRC64;
MKSFNPPVRT LMGPGPSDVH PRILSAMARP TIGHLDPAFV GMMNETKEGL KYIFQTENEL
TMPVSAPGSA GMETCFANLV EPGDKVVVCI NGVFGMRMQE NITRFGGEAI VVEDAWGSAV
STDKVEQALK ENPDAKILAF VHAETSTGAQ SDAKTLCKIA HENDCITIVD AVTSLAGSEL
RVDEWEIDAI YSGTQKCLSA MPGISPVSFN ERALAKVRNR KTAVTSWFLD LNLVMGYWGE
GAKRTYHHTA PVNTLYGLHE SLVMLSEEGL ENSWARHQKN HEELRDGLEA MGINFLVDKA
DRLPQLNSVF IPEGVDDVAV RATLLNDYNL EIGAGLGAYA GKVWRIGLMG HSSRKENITL
CLAALKATLE K
//
