ID   GSA2_CENSY              Reviewed;         434 AA.
AC   O74038; A0RWS6;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase 2;
DE            Short=GSA 2;
DE            EC=5.4.3.8;
DE   AltName: Full=Glutamate-1-semialdehyde aminotransferase 2;
DE            Short=GSA-AT 2;
GN   Name=hemL2; Synonyms=gsaT; OrderedLocusNames=CENSYa_1168;
OS   Cenarchaeum symbiosum (strain A).
OC   Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=414004;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=9748430; DOI=10.1128/jb.180.19.5003-5009.1998;
RA   Schleper C., Delong E.F., Preston C.M., Feldman R.A., Wu K.-Y.,
RA   Swanson R.V.;
RT   "Genomic analysis reveals chromosomal variation in natural populations of
RT   the uncultured psychrophilic archaeon Cenarchaeum symbiosum.";
RL   J. Bacteriol. 180:5003-5009(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-4-amino-5-oxopentanoate = 5-aminolevulinate;
CC         Xref=Rhea:RHEA:14265, ChEBI:CHEBI:57501, ChEBI:CHEBI:356416;
CC         EC=5.4.3.8;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily. {ECO:0000305}.
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DR   EMBL; AF083071; AAC62681.1; -; Genomic_DNA.
DR   EMBL; DP000238; ABK77793.1; -; Genomic_DNA.
DR   AlphaFoldDB; O74038; -.
DR   SMR; O74038; -.
DR   STRING; 414004.CENSYa_1168; -.
DR   EnsemblBacteria; ABK77793; ABK77793; CENSYa_1168.
DR   KEGG; csy:CENSYa_1168; -.
DR   PATRIC; fig|414004.10.peg.1061; -.
DR   HOGENOM; CLU_016922_1_5_2; -.
DR   OMA; NFGMVEP; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000000758; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Porphyrin biosynthesis; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN           1..434
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase 2"
FT                   /id="PRO_0000120478"
FT   MOD_RES         267
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   434 AA;  46714 MW;  D1ED70D39A25CA50 CRC64;
     MDLEREYRAK TGGSARIFAR SKKYHVGGVS HNIRFYEPYP FVTRSASGKH LVDVDGNKYV
     DYWMGHWSLI LGHAPAPVRS AVEGQLRRGW IHGTVNEQTM NLSEIIRGAV SVAEKTRYVT
     SGTEAVMYAA RLARAHTGRK IIAKADGGWH GYASGLLKSV NWPYDVPESG GLVDEEHSIS
     IPYNDLEGSL DVLGRAGDDL ACVIIEPLLG GGGCIPADED YLRGIQEFVH SRGALLVLDE
     IVTGFRFRFG CAYAAAGLDP DIVALGKIVG GGFPIGVICG KDEVMEISNT ISHAKSDRAY
     IGGGTFSANP ATMTAGAAAL GELKKRKGTI YPRINSMGDD ARDKLSKIFG NRVSVTGRGS
     LFMTHFVQDG AGRVSNAADA AACDVELLHR YHLDMITRDG IFFLPGKLGA ISAAHSKADL
     KTMYSASERF AEGL