ID   SGAA_METEA              Reviewed;         402 AA.
AC   P55819; C5B106;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Serine--glyoxylate aminotransferase {ECO:0000305};
DE            Short=SGAT {ECO:0000303|PubMed:8144463};
DE            EC=2.6.1.45 {ECO:0000269|PubMed:8144463};
GN   Name=sgaA {ECO:0000303|PubMed:8144463};
GN   OrderedLocusNames=MexAM1_META1p1726;
OS   Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS   9133 / AM1) (Methylobacterium extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=272630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX   PubMed=8144463; DOI=10.1128/jb.176.7.1957-1968.1994;
RA   Chistoserdova L.V., Lidstrom M.E.;
RT   "Genetics of the serine cycle in Methylobacterium extorquens AM1:
RT   identification of sgaA and mtdA and sequences of sgaA, hprA, and mtdA.";
RL   J. Bacteriol. 176:1957-1968(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX   PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA   Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA   Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA   Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA   Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA   Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA   Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA   Lidstrom M.E.;
RT   "Methylobacterium genome sequences: a reference blueprint to investigate
RT   microbial metabolism of C1 compounds from natural and industrial sources.";
RL   PLoS ONE 4:E5584-E5584(2009).
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:8144463};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:Q988B8};
CC   -!- PATHWAY: One-carbon metabolism; formaldehyde assimilation via serine
CC       pathway. {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Mutants cannot grow on Cl compounds (methanol,
CC       methylamine, and formate) but grow normally on C2 compounds (ethanol
CC       and ethylamine). {ECO:0000269|PubMed:8144463}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; L27235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP001510; ACS39570.1; -; Genomic_DNA.
DR   RefSeq; WP_003597639.1; NC_012988.1.
DR   AlphaFoldDB; P55819; -.
DR   SMR; P55819; -.
DR   STRING; 272630.MexAM1_META1p1726; -.
DR   EnsemblBacteria; ACS39570; ACS39570; MexAM1_META1p1726.
DR   KEGG; mea:Mex_1p1726; -.
DR   eggNOG; COG0075; Bacteria.
DR   HOGENOM; CLU_027686_1_0_5; -.
DR   OMA; AHMGHVN; -.
DR   OrthoDB; 996960at2; -.
DR   UniPathway; UPA00927; -.
DR   Proteomes; UP000009081; Chromosome.
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; 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   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000524; SPT; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..402
FT                   /note="Serine--glyoxylate aminotransferase"
FT                   /id="PRO_0000150233"
FT   MOD_RES         201
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q988B8"
FT   CONFLICT        1..6
FT                   /note="MAATRR -> M (in Ref. 1; L27235)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        176..193
FT                   /note="Missing (in Ref. 1; L27235)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   402 AA;  43182 MW;  71B25D3180DB9443 CRC64;
     MAATRRPGRN HLFVPGPTNI PDRVMRAMMV QSEDHRSVDF PSLTKPLFED TKKVFGSTEG
     TIFLFPASGT GIWESALSNT LARGDKVLAA RFGQFSHLWI DMAQRLGLDV VVQEEEWGTG
     AKPEKIEEAL RADKNHEIKA VMVVHNETAT GVTSNIGAVR KAIDAAGHPA LLFVDGVSSI
     GSLPFKADEW KVDCAIAGSQ KGLMLPAGLG VICVSQKALK AAEGQSGRND RLARVYFDWE
     DQKKQNPTGY FPYTPPLPLL YGLREALACL FEEGLENVYH RHAVLGEATR QAVAAWGLKT
     CAKSPEWNSD TVTAILAPEG VDAAKIIKHA YVRYNLALGA GLSQVAGKVF RIGHVGDLNE
     LSLLGAIAGA EMSLIDNGVK VTPGSGVAAA SSYLRENPLA KA