ID A0A0K8JH13_9FIRM Unreviewed; 434 AA.
AC A0A0K8JH13;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Alanine-glyoxylate aminotransferase 2 homolog 1, mitochondrial {ECO:0000313|EMBL:CUH96892.1};
DE EC=2.6.1.44 {ECO:0000313|EMBL:CUH96892.1};
GN Name=AGT2 {ECO:0000313|EMBL:CUH96892.1};
GN ORFNames=P22_3004 {ECO:0000313|EMBL:CUH96892.1};
OS Propionispora sp. 2/2-37.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Propionispora.
OX NCBI_TaxID=1677858 {ECO:0000313|EMBL:CUH96892.1, ECO:0000313|Proteomes:UP000041641};
RN [1] {ECO:0000313|EMBL:CUH96892.1, ECO:0000313|Proteomes:UP000041641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2/2 {ECO:0000313|EMBL:CUH96892.1};
RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CYSP01000014; CUH96892.1; -; Genomic_DNA.
DR RefSeq; WP_054261027.1; NZ_CYSP01000014.1.
DR AlphaFoldDB; A0A0K8JH13; -.
DR STRING; 1677858.P22_3004; -.
DR OrthoDB; 3034088at2; -.
DR Proteomes; UP000041641; Unassembled WGS sequence.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CUH96892.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000041641};
KW Transferase {ECO:0000313|EMBL:CUH96892.1}.
SQ SEQUENCE 434 AA; 47410 MW; 590DFB91A5DAC721 CRC64;
MSKYIGVSEV LRKKRDYLIP CVYHFYKEPM QIVRGEMQYL YDDQGKQYLD CFAGVSVVNC
GHCNPDITKA ICKQVTTLQH TCTIYLTENI VNLAERLAQI TPGQLQKSFF CASGSEANEG
AALLASIYTG KHEFISLRQG LHGRTKLGMS LTGLGMWRTD SSPVGGIAFA PNAYCYRCPF
QKQYPECDLA CANELETVIK TTTSGQVAAM FVEPIQGNGG IITPPPGYFK RLKEILNQYG
ILLIVDEVQT GFGRTGKMFA IEHYETNPDI MTVAKALANG TPVGAFITTS PIADTYTRPG
ASTLGGNPVT STAALATLDF ILRNDLPAKA AYLGTYLKDG LLTLQKKHPV IGDVRGLGLM
LGAELVHADK SPAAQEMDTI QEQLKNRGFL VGKNGPDRNV LALQPPLVIT QTDIDHLLNN
LEDVLSLLTT HKPR
//
