ID H2J2X0_MARPK Unreviewed; 365 AA.
AC H2J2X0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Putative PLP-dependent enzyme possibly involved in cell wall biogenesis {ECO:0000313|EMBL:AEX85661.1};
GN OrderedLocusNames=Marpi_1257 {ECO:0000313|EMBL:AEX85661.1};
OS Marinitoga piezophila (strain DSM 14283 / JCM 11233 / KA3).
OC Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC Marinitoga.
OX NCBI_TaxID=443254 {ECO:0000313|EMBL:AEX85661.1, ECO:0000313|Proteomes:UP000007161};
RN [1] {ECO:0000313|EMBL:AEX85661.1, ECO:0000313|Proteomes:UP000007161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14283 / JCM 11233 / KA3
RC {ECO:0000313|Proteomes:UP000007161};
RX PubMed=23045491; DOI=10.1128/JB.01430-12;
RA Lucas S., Han J., Lapidus A., Cheng J.F., Goodwin L.A., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N.C., Ivanova N., Pagani I., Vannier P.,
RA Oger P., Bartlett D.H., Noll K.M., Woyke T., Jebbar M.;
RT "Complete Genome Sequence of the Thermophilic, Piezophilic, Heterotrophic
RT Bacterium Marinitoga piezophila KA3.";
RL J. Bacteriol. 194:5974-5975(2012).
RN [2] {ECO:0000313|Proteomes:UP000007161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14283 / JCM 11233 / KA3
RC {ECO:0000313|Proteomes:UP000007161};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Jebbar M.,
RA Vannier P., Oger P., Cario A., Bartlett D., Noll K.M., Woyke T.;
RT "Complete sequence of chromosome of Marinitoga piezophila KA3.";
RL Submitted (JAN-2012) 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}.
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DR EMBL; CP003257; AEX85661.1; -; Genomic_DNA.
DR RefSeq; WP_014296732.1; NC_016751.1.
DR AlphaFoldDB; H2J2X0; -.
DR STRING; 443254.Marpi_1257; -.
DR KEGG; mpz:Marpi_1257; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_2_4_0; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000007161; Chromosome.
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; IPR026385; LegC-like.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR04181; NHT_00031; 1.
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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000007161}.
FT ACT_SITE 184
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 184
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 365 AA; 41148 MW; FE21E257C45A68B3 CRC64;
MKNEILLDAP NLGELEKEYL IKCIDSTFVS TAGPFIPEFE EKFAKYVGTK RAVSVQSGTA
ALYMALYELG IGPGDEVIVP VITFIASVNP IMYLGATPVF VDVDPETWNI DPKEVEKAIT
KNTKAIIPVH LYGNPCDMDG LMYISKKYGI PIIEDATESL GATYNGKMTG TFGILNAFSF
NGNKIMTTGG GGMITTNDEE KAEHIKFLIN QARDASRGYY HPEIGFNYRM TNLEASLGLA
QLERLEEFLN KKRRFAKIYM ENLQDVKEIK FQKEYENAES SWWLTSIKIN SDKSISEIQS
ELKEKGIPTR RIFVPIVEFP PYQKFKTSNY KNAYEIYERG LNLPSSTVNG YDSIKFVAEE
LKNVI
//
