ID A0A0N0GNG6_9NEIS Unreviewed; 373 AA.
AC A0A0N0GNG6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Putative 8-amino-7-oxononanoate synthase {ECO:0000256|ARBA:ARBA00021531};
GN Name=epsN {ECO:0000313|EMBL:KPC52695.1};
GN ORFNames=WG78_12645 {ECO:0000313|EMBL:KPC52695.1};
OS Amantichitinum ursilacus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Amantichitinum.
OX NCBI_TaxID=857265 {ECO:0000313|EMBL:KPC52695.1, ECO:0000313|Proteomes:UP000037939};
RN [1] {ECO:0000313|EMBL:KPC52695.1, ECO:0000313|Proteomes:UP000037939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGB-41 {ECO:0000313|EMBL:KPC52695.1,
RC ECO:0000313|Proteomes:UP000037939};
RA Kirstahler P., Guenther M., Grumaz C., Rupp S., Zibek S., Sohn K.;
RT "Draft genome sequence of the Amantichitinum ursilacus IGB-41, a new
RT chitin-degrading bacterium.";
RL Submitted (JUL-2015) 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 DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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:KPC52695.1}.
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DR EMBL; LAQT01000009; KPC52695.1; -; Genomic_DNA.
DR RefSeq; WP_053938168.1; NZ_LAQT01000009.1.
DR AlphaFoldDB; A0A0N0GNG6; -.
DR STRING; 857265.WG78_12645; -.
DR PATRIC; fig|857265.3.peg.2606; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000037939; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KPC52695.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000037939};
KW Transferase {ECO:0000313|EMBL:KPC52695.1}.
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 185
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 373 AA; 40838 MW; 3E303DA4AF8D77F5 CRC64;
MSQDRILYTK PSITALEVQY ATDAAANGWG EHCYDYLNRF EREFAAWMGV PHAIATSSCT
GAMHMGLAAL DIGAGDEVIL ADTNWIATVA PIVHVGATPV FVDVLIDSWC IDPQAVRAAI
TPRTKAIVAT HLYGNLCALD ELAALAEQHG LALIEDAAEA IGSVYHGRRA GASARFGVFS
FHGTKTMTTG EGGMFVTSDA DLYERVLTLS NHGRKRGETK QFWPSEVGFK YKMSNLQAAL
GCAQLSRIDE LVRRKREVFQ HYQQRLQPYV DKGVLAINPE AANTQNGYWM PTVVFASATG
ITRERLQQAF KTEDIDARVF FSPLSSTPSF SPVATNTLAY DLPHRAINLP SYHDLTEPQI
ARVVACLLSV LPD
//
