ID A0A431U1M8_9BACT Unreviewed; 457 AA.
AC A0A431U1M8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000313|EMBL:RTQ48966.1};
DE EC=5.4.3.8 {ECO:0000313|EMBL:RTQ48966.1};
GN ORFNames=EJV47_15345 {ECO:0000313|EMBL:RTQ48966.1};
OS Hymenobacter gummosus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1776032 {ECO:0000313|EMBL:RTQ48966.1, ECO:0000313|Proteomes:UP000282184};
RN [1] {ECO:0000313|EMBL:RTQ48966.1, ECO:0000313|Proteomes:UP000282184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 52166 {ECO:0000313|EMBL:RTQ48966.1,
RC ECO:0000313|Proteomes:UP000282184};
RA Nie L.;
RT "Hymenobacter gummosus sp. nov., isolated from a spring.";
RL Submitted (DEC-2018) 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:RTQ48966.1}.
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DR EMBL; RXOF01000008; RTQ48966.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A431U1M8; -.
DR OrthoDB; 9762089at2; -.
DR Proteomes; UP000282184; Unassembled WGS sequence.
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 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; IPR049704; Aminotrans_3_PPA_site.
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.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:RTQ48966.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 50110 MW; 4B325CCBF8964CB1 CRC64;
MDPLLTSAPP ATAAPPSFAH TPRRFDASVA LGPRFHQLIP GGAHTYAKGD DQWAEHMAPY
LVRGQGCHVW DVDGNQFVEY NAGLRSVTLG HAYPAVVRAA QRQMELGTNF GRPAVLELEL
AEEFLDFTGA GDMVKFAKNG SDVTSAAVKL ARAYTGRDLV AICHDHPFFS VDDWFIGSTP
LQAGVPRAVQ QLTVSFRYND LGSLQVLVDQ YPGQLACVVM EVEKDTPPAE GFLPGVQALC
RREGIVLIFD EIITGLRWHN RGAQGLHGVQ PDLSTWGKAL GNGFSIAALA GRRELMERGG
LQHPHERVFL LSTTYGSESH ALAAARAVLH TYRTEPVVEQ LHAHGERLAR GMNQAIQAHG
LQPYVQVLGR PCCLTFATRD GQGQPSQALR ALFLQEMTRR GVLCPSFVTN YSLTDAIVDE
TVASIYEALA IYRRALDEGV GRYLEGRPLK VVYRRYN
//
