ID   E6PI07_9ZZZZ            Unreviewed;       397 AA.
AC   E6PI07;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Glutamate-1-semialdehyde 2,1-aminomutase (GSA) (Glutamate-1-semialdehyde aminotransferase) (GSA-AT) {ECO:0000313|EMBL:CBH76097.1};
DE            EC=5.4.3.8 {ECO:0000313|EMBL:CBH76097.1};
GN   Name=hemL {ECO:0000313|EMBL:CBH76097.1};
GN   ORFNames=CARN1_0577 {ECO:0000313|EMBL:CBH76097.1};
OS   mine drainage metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=410659 {ECO:0000313|EMBL:CBH76097.1};
RN   [1] {ECO:0000313|EMBL:CBH76097.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Bertin P.N., Heinrich-Salmeron A., Pelletier E., Goulhen-Chollet F.,
RA   Arsene-Ploetze F., Gallien S., Calteau A., Vallenet D., Casiot C.,
RA   Chane-Woon-Ming B., Giloteaux L., Barakat M., Bonnefoy V., Bruneel O.,
RA   Chandler M., Cleiss J., Duran R., Elbaz-Poulichet F., Fonknechten N.,
RA   Lauga B., Mornico D., Ortet P., Schaeffer C., Siguier P.,
RA   Alexander Thil Smith A., Van Dorsselaer A., Weissenbach J., Medigue C.,
RA   Le Paslier D.;
RT   "Diversity of trophic interactions inside an arsenic-rich microbial
RT   ecosystem.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:CBH76097.1}.
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DR   EMBL; CABL01000019; CBH76097.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6PI07; -.
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:UniProtKB-KW.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR   PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000313|EMBL:CBH76097.1};
KW   Isomerase {ECO:0000313|EMBL:CBH76097.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Transferase {ECO:0000313|EMBL:CBH76097.1}.
SQ   SEQUENCE   397 AA;  43032 MW;  0D0CB2FE640034B3 CRC64;
     MFVQAGAQGA YAYDERGRRY IDYIMGYGPL LFGHTHPALV TDLDALAANG WMWGTTHPEE
     VRLAERIRGY LPAMERLRFA TTGTEAVMGA IRVARASTRR STIVKFAGNY HGHSDLALFD
     AGASAHTDDA VRSGIPRGVT QDVIVARYND LDDLDAKVRG RESEVAAILV EPIVGNMGYV
     TPVPGFLAGL RARADRYGAL LMFDEVITWL RLGLHGASAL VGVTPDLVTV GKILGGGAPI
     AAFGGRAEVM AELAPDGRVF TGGTHAGNPF AVGMAHRVLD LLESHPQYYA QMERLAVQLA
     DGIRALFAAR ALPYAVVQHA SIVDFKFRAG EPNRNFDDAL RADKQLYRRY YEAMFARGIL
     LPPSQNEVMF LSVAHGQGDV EATLVAIGES LDEIFTN
//