ID A0A0S8BI38_9PROT Unreviewed; 375 AA.
AC A0A0S8BI38;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Alanine--glyoxylate aminotransferase {ECO:0000313|EMBL:KPK10852.1};
GN ORFNames=AMJ68_07925 {ECO:0000313|EMBL:KPK10852.1};
OS Acidithiobacillales bacterium SG8_45.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales.
OX NCBI_TaxID=1703383 {ECO:0000313|EMBL:KPK10852.1, ECO:0000313|Proteomes:UP000053136};
RN [1] {ECO:0000313|EMBL:KPK10852.1, ECO:0000313|Proteomes:UP000053136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_45 {ECO:0000313|EMBL:KPK10852.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(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}.
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:KPK10852.1}.
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DR EMBL; LJTU01000035; KPK10852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8BI38; -.
DR PATRIC; fig|1703383.3.peg.973; -.
DR Proteomes; UP000053136; Unassembled WGS sequence.
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:KPK10852.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Transferase {ECO:0000313|EMBL:KPK10852.1}.
FT DOMAIN 34..320
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 180
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 375 AA; 40196 MW; 6068CBAC4D769F39 CRC64;
MTTKSFVPPL RTLMGPGPSD VHPRILEAMA KAMLQYAFQT KNELTIPVSA PGSAGMETCF
VNLIEPGDKV IVCQNGVFGG RMKENVERAG GMAVMVEDEW GTAVDPDKLE QALKKNPDAK
IVAFVHAETS TGVQSDAKTL CEIAHKHDCL TIVDTVTSLG GTPVLVDDWG IDAVYSGTQK
CLSCTPGLSP VSFSDQAVAA IKARKTRVHS WFLDLNLVMG YWGSGQAKRA YHHTAPINAL
YGLHESLVML EEEGLENAWA RHQRNHQALR AGIEAMGLSF LVTEAHRLPQ LNAIVIPEGI
DEAAVRARLL SEFDLEIGAG LGALAGKVWR IGLMGHASNM KNIMFCLGAM ESILSEMNVP
ISGGAITAAQ KAAIA
//
