ID G9PQ36_9ACTO Unreviewed; 300 AA.
AC G9PQ36;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Glutamate-1-semialdehyde-2,1-aminomutase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=HMPREF0975_02507 {ECO:0000313|EMBL:EHM91352.1};
OS Actinomyces sp. oral taxon 849 str. F0330.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=653386 {ECO:0000313|EMBL:EHM91352.1, ECO:0000313|Proteomes:UP000003600};
RN [1] {ECO:0000313|EMBL:EHM91352.1, ECO:0000313|Proteomes:UP000003600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0330 {ECO:0000313|EMBL:EHM91352.1,
RC ECO:0000313|Proteomes:UP000003600};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V.,
RA Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C.,
RA Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Actinomyces sp. oral taxon 849 str. F0330.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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:EHM91352.1}.
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DR EMBL; ACTB01000160; EHM91352.1; -; Genomic_DNA.
DR AlphaFoldDB; G9PQ36; -.
DR STRING; 653386.HMPREF0975_02507; -.
DR PATRIC; fig|653386.3.peg.2331; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_062345_0_0_11; -.
DR Proteomes; UP000003600; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
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); 2.
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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000003600}.
FT REGION 92..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHM91352.1"
SQ SEQUENCE 300 AA; 30751 MW; 2C4192DC594BB791 CRC64;
VLPYNDVAAL EACFAERGSE IAAVITEGAP ANMGIVPPAP GFNAAIRRVT AEHGALMILD
EVLTGFRVGP AGWWGLEAVD GWTSDLPAFA AEPSTAGATS SEPADAAAPS WPGADWRERA
TWVPDLVTFG KVVGGGMPLA AVGGRAEVMD LLAPGGPVYQ AGTLSGNPLA TAAGLATLQL
ADDAVYASVA EHAQAISKVV SAALSEQGVP HRVQRAGSLF SLMFGPQAAE RGVADYEAAR
AQETWRYGPF FHAFLEAGVS LPPSVFEAWF VSAAHGEAEL EAIAAAAPAA ARAAARAQEH
//
