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Database: UniProt
Entry: U7NVM0_9GAMM
LinkDB: U7NVM0_9GAMM
Original site: U7NVM0_9GAMM 
ID   U7NVM0_9GAMM            Unreviewed;       430 AA.
AC   U7NVM0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000256|HAMAP-Rule:MF_00375};
DE            Short=GSA {ECO:0000256|HAMAP-Rule:MF_00375};
DE            EC=5.4.3.8 {ECO:0000256|HAMAP-Rule:MF_00375};
DE   AltName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000256|HAMAP-Rule:MF_00375};
DE            Short=GSA-AT {ECO:0000256|HAMAP-Rule:MF_00375};
GN   Name=hemL {ECO:0000256|HAMAP-Rule:MF_00375};
GN   ORFNames=Q671_08660 {ECO:0000313|EMBL:ERS86494.1};
OS   Halomonas sp. PBN3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1397528 {ECO:0000313|EMBL:ERS86494.1, ECO:0000313|Proteomes:UP000017115};
RN   [1] {ECO:0000313|EMBL:ERS86494.1, ECO:0000313|Proteomes:UP000017115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBN3 {ECO:0000313|EMBL:ERS86494.1,
RC   ECO:0000313|Proteomes:UP000017115};
RX   PubMed=24356826;
RA   Overholt W.A., Green S.J., Marks K.P., Venkatraman R., Prakash O.,
RA   Kostka J.E.;
RT   "Draft genome sequences for oil-degrading bacterial strains from beach
RT   sands impacted by the deepwater horizon oil spill.";
RL   Genome Announc. 1:e01015-13(2013).
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; Evidence={ECO:0000256|HAMAP-Rule:MF_00375};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_00375};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC       {ECO:0000256|ARBA:ARBA00004819}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00375}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00375}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily.
CC       {ECO:0000256|ARBA:ARBA00008981, ECO:0000256|HAMAP-Rule:MF_00375}.
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:ERS86494.1}.
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DR   EMBL; AXCA01000166; ERS86494.1; -; Genomic_DNA.
DR   RefSeq; WP_023006387.1; NZ_AXCA01000166.1.
DR   AlphaFoldDB; U7NVM0; -.
DR   PATRIC; fig|1397528.3.peg.2186; -.
DR   eggNOG; COG0001; Bacteria.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000017115; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-UniRule.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_00375; HemL_aminotrans_3; 1.
DR   InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase.
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   NCBIfam; TIGR00713; hemL; 1.
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.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00375};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00375};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP-
KW   Rule:MF_00375};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_00375}.
FT   MOD_RES         265
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   430 AA;  45600 MW;  085B5543E5ACBA7A CRC64;
     MTTSAELFAQ ACRHIPGGVN SPVRAFKGLQ RPPVFMERAQ GAYLFDVEGK RYVDYVGSWG
     PMITGHADPE VLGAVRSRLD GGLSFGTPTA IETTMADLIC EMIPSIEMVR MVNSGTEATM
     SAIRLARGVT GRDKIIKFEG NYHGHSDSLL VKAGSGALTH GEPSSPGVPA SLAEHTVTLA
     YNDIDAVEQC FEEIGDQVAC IIVEPVAGNM NCIPPQPGFL KSLRRVCDAH DSVLIFDEVM
     TGFRVAMGGA QAHYGVCPDL TCLGKIVGGG MPVGAFGGSE AIMSNISPLG PIYQAGTLSG
     NPLAMAAGIA LLTKLREPGF HDALAQRVET LCHGLQERAD AAGVEMITQR AGGMFGLFFT
     GQSRVDNFAQ ATACDADAFR RFFSAMLDEG VYLAPSAYEA GFMSSAHTPE DIQFTLDAAE
     KAFDAMQREA
//
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