ID A0A1F4Q8A7_9BACT Unreviewed; 425 AA.
AC A0A1F4Q8A7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3H39_17440 {ECO:0000313|EMBL:OGB92253.1};
OS candidate division NC10 bacterium RIFCSPLOWO2_02_FULL_66_22.
OC Bacteria; candidate division NC10.
OX NCBI_TaxID=1801658 {ECO:0000313|EMBL:OGB92253.1, ECO:0000313|Proteomes:UP000177374};
RN [1] {ECO:0000313|EMBL:OGB92253.1, ECO:0000313|Proteomes:UP000177374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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:OGB92253.1}.
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DR EMBL; METH01000122; OGB92253.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4Q8A7; -.
DR STRING; 1801658.A3H39_17440; -.
DR Proteomes; UP000177374; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
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 PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}.
SQ SEQUENCE 425 AA; 45697 MW; 4F9EB1C9FF8DDB65 CRC64;
MPTLSERSLA VFPAGSPGEY NLPPDLVTVL DRGEGAAVWD AAGRRFLDFT MGWGSVLLGH
AHPAVVEAVR RRAGLGSNFA YVTEPALELA EELVRAVACA ERVRFCASGT EATSYAVRLA
RAYTGRPKVL KFEGAYHGGN AIGTVSLFPS RLVDFPEGEP SSAGLAPGAV ADILVAPYND
LGTTRAIVAE HRHVLAAIIV EPLHRCTPPR PDFLQGLREL TAEFGLLLIF DETVTGFRLA
YGGAQEYYGI RPDLAALGKA LGGGYPIGAV VGRADVLDLV REDRMGQERY VWFASSLGGN
PVSAAAALAT LAELRKPGTY ERLFALGEAL RSGLRAVLRD EGVTAHVQGD GPLGAVLFTD
REVVDYRTAF GADRKRARAF TLGLFRRGIF LNPMSTKLYL SLAHTEADIR EFLEVARATL
REACR
//
