ID K8GGY8_9CYAN Unreviewed; 383 AA.
AC K8GGY8;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Serine-pyruvate aminotransferase/archaeal aspartate aminotransferase {ECO:0000313|EMBL:EKQ68193.1};
DE EC=2.6.1.44 {ECO:0000313|EMBL:EKQ68193.1};
DE Flags: Precursor;
GN ORFNames=OsccyDRAFT_2715 {ECO:0000313|EMBL:EKQ68193.1};
OS Leptolyngbyaceae cyanobacterium JSC-12.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae.
OX NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ68193.1, ECO:0000313|Proteomes:UP000001332};
RN [1] {ECO:0000313|EMBL:EKQ68193.1, ECO:0000313|Proteomes:UP000001332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ68193.1,
RC ECO:0000313|Proteomes:UP000001332};
RG DOE Joint Genome Institute;
RA Brown I., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RT "Improved high quality draft of Oscillatoriales sp. JSC-12.";
RL Submitted (OCT-2012) 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}.
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:EKQ68193.1}.
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DR EMBL; AJUB01000011; EKQ68193.1; -; Genomic_DNA.
DR AlphaFoldDB; K8GGY8; -.
DR STRING; 864702.OsccyDRAFT_2715; -.
DR PATRIC; fig|864702.5.peg.2919; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_027686_0_0_3; -.
DR OrthoDB; 389074at2; -.
DR Proteomes; UP000001332; Chromosome.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
DR CDD; cd06451; AGAT_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; 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:EKQ68193.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50}; Pyruvate {ECO:0000313|EMBL:EKQ68193.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001332};
KW Transferase {ECO:0000313|EMBL:EKQ68193.1}.
FT DOMAIN 47..365
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 383 AA; 42354 MW; F2BCE1CCA23F4CE3 CRC64;
MTETISIRDR HRLRLAPLRV PERLLLGPGP SNAHPTVLQA MSTIPLGHLD PDFLGIMDEI
QLLLRYIWQT DNPMTIAISG TGSAAMEATI ANSVEPGDVV LVGVMGYFGN RLVDMAERYG
ADVRTITKPW GHVFSLTELR TAMETHRPAI LALVHAETST GAHQPLEGVG ELCREFGCLL
LVDMVTSLGG VPIFLDEWGV DLAYSCSQKG LGCSPGASPF TMSPRAIEKL QNRKTKVANW
YLDARLLGKY WGSDRVYHHT APINLYYGLR EALRLVAEEG LAACWQRHQR NVEYLWQRLE
EIGLALHVER EFRLPTLTTV RVPDGVDAKA IARTLLLEHN IEIGGGLGEL AGKVWRVGLM
GYNSKPESVD RLIDALKLVL GKP
//
