ID C7MSW2_SACVD Unreviewed; 387 AA.
AC C7MSW2;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Succinyldiaminopimelate aminotransferase {ECO:0000313|EMBL:ACU95323.1};
GN OrderedLocusNames=Svir_02410 {ECO:0000313|EMBL:ACU95323.1};
OS Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 / NBRC
OS 12207 / P101).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=471857 {ECO:0000313|EMBL:ACU95323.1, ECO:0000313|Proteomes:UP000000841};
RN [1] {ECO:0000313|EMBL:ACU95323.1, ECO:0000313|Proteomes:UP000000841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101
RC {ECO:0000313|Proteomes:UP000000841};
RX PubMed=21304650; DOI=10.4056/sigs.20263;
RA Pati A., Sikorski J., Nolan M., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA Goodwin L., Chain P., D'haeseleer P., Chen A., Palaniappan K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Rohde M., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Saccharomonospora viridis type strain
RT (P101).";
RL Stand. Genomic Sci. 1:141-149(2009).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; CP001683; ACU95323.1; -; Genomic_DNA.
DR RefSeq; WP_012795756.1; NC_013159.1.
DR AlphaFoldDB; C7MSW2; -.
DR STRING; 471857.Svir_02410; -.
DR KEGG; svi:Svir_02410; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_0_11; -.
DR Proteomes; UP000000841; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_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 InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43807; FI04487P; 1.
DR PANTHER; PTHR43807:SF20; FI04487P; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000313|EMBL:ACU95323.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000841};
KW Transferase {ECO:0000313|EMBL:ACU95323.1}.
FT DOMAIN 30..383
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 387 AA; 41702 MW; D34A1C7AF598CED0 CRC64;
MREPVLVERM RPFTSTIFAE MTALADRTSA VNLGQGFPDT DGPAGMLDAA RDALFGGANQ
YPPGPGLPEL REAIAKHRAR YGTEYDPERE ILVTAGATEA IAASLLALTG PGDEVIVIEP
YYDSYAAAVA MAGATRRVVS LVPDGDRFAL DLDAVRAAVG PKTRAVLVNS PHNPTGTVFT
RAELAELAQV CVEHDLIAIT DEVYEHLTFD GAEHLPLAGF PGMSSRTVTI SSAGKTFNCT
GWKIGWVCAA PELVSAVRAV KQFLTFVSGG PFQPAVAHAL RHELSWVESL RESLQAKRDR
LCAGLAEAGF AVRPSAGTYF VCADVRPLGF TDAEELAWRL PESIGVATVP VSVFTDHPKA
WNHLLRFAFC KREEVLDEAI QRLRTLS
//
