ID   SGAA_HYPME              Reviewed;         405 AA.
AC   O08374;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Serine--glyoxylate aminotransferase {ECO:0000303|PubMed:8898880};
DE            Short=SGAT {ECO:0000305};
DE            EC=2.6.1.45 {ECO:0000269|PubMed:8898880};
GN   Name=sgaA;
OS   Hyphomicrobium methylovorum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Hyphomicrobium.
OX   NCBI_TaxID=84;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-40, CATALYTIC
RP   ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=GM2;
RX   PubMed=8898880; DOI=10.1111/j.1432-1033.1996.0001t.x;
RA   Hagishita T., Yoshida T., Izumi Y., Mitsunaga T.;
RT   "Cloning and expression of the gene for serine-glyoxylate aminotransferase
RT   from an obligate methylotroph Hyphomicrobium methylovorum GM2.";
RL   Eur. J. Biochem. 241:1-5(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glyoxylate + L-serine = 3-hydroxypyruvate + glycine;
CC         Xref=Rhea:RHEA:19125, ChEBI:CHEBI:17180, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:36655, ChEBI:CHEBI:57305; EC=2.6.1.45;
CC         Evidence={ECO:0000269|PubMed:8898880};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:Q988B8};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.68 mM for glyoxylate {ECO:0000269|PubMed:8898880};
CC         KM=3.86 mM for L-serine {ECO:0000269|PubMed:8898880};
CC   -!- PATHWAY: One-carbon metabolism; formaldehyde assimilation via serine
CC       pathway. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D86125; BAA19919.1; -; Genomic_DNA.
DR   AlphaFoldDB; O08374; -.
DR   SMR; O08374; -.
DR   BioCyc; MetaCyc:MON-4229; -.
DR   UniPathway; UPA00927; -.
DR   GO; GO:0050281; F:serine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
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   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000524; SPT; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Direct protein sequencing; Pyridoxal phosphate;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8898880"
FT   CHAIN           2..405
FT                   /note="Serine--glyoxylate aminotransferase"
FT                   /id="PRO_0000150232"
FT   MOD_RES         196
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q988B8"
SQ   SEQUENCE   405 AA;  43894 MW;  D27DC5B69853FA52 CRC64;
     MTVTPHLFIP GPTNIPDAVR MAMNIPMEDM RSPEFPKFTL PLFEDLKKAF KMKDGRVFIF
     PSSGTGAWES AVENTLATGD KVLMSRFGQF SLLWVDMCER LGLKVEVCDE EWGTGVPVEK
     YADILAKDKN HEIKAVFVTH NETATGVSSD VAGVRKALDA AKHPALLMVD GVSSVGSLDM
     RMGEWGVDCC VSGSQKGFML PTGLGILAVS QKALDINKSK NGRMNRCFFS FEDMIKTNDQ
     GFFPYTPATQ LLRGLRTSLD LLFAEGLDNV FARHTRLASG VRAAVDAWGL KLCAKEPKWY
     SDTVSAILVP EGIDSNAITK TAYYRYNTSF GLGLNKVAGK VFRIGHLGML DEVMIGGALF
     AAEMALKDNG VNLKLGSGTG AAAEYFSKNA TKSATALTPK QAKAA