ID C4ICV7_CLOBU Unreviewed; 392 AA.
AC C4ICV7;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=Putative pleiotropic regulatory protein DegT {ECO:0000313|EMBL:EEP55871.1};
GN ORFNames=CLP_3183 {ECO:0000313|EMBL:EEP55871.1};
OS Clostridium butyricum E4 str. BoNT E BL5262.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=632245 {ECO:0000313|EMBL:EEP55871.1, ECO:0000313|Proteomes:UP000003081};
RN [1] {ECO:0000313|EMBL:EEP55871.1, ECO:0000313|Proteomes:UP000003081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E4 str. BoNT E BL5262 {ECO:0000313|Proteomes:UP000003081};
RA Shrivastava S., Brinkac L.B., Brown J.L., Bruce D.B., Detter C.,
RA Green L.D., Munk C.A., Rogers Y.C., Tapia R., Sims D.R., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {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:EEP55871.1}.
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DR EMBL; ACOM01000002; EEP55871.1; -; Genomic_DNA.
DR RefSeq; WP_003413818.1; NZ_ACOM01000002.1.
DR AlphaFoldDB; C4ICV7; -.
DR STRING; 1492.ATN24_00230; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_6_0_9; -.
DR Proteomes; UP000003081; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 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|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000003081}.
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 186
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 392 AA; 43520 MW; 3D4C617159911BD4 CRC64;
MNIPLIDLKA QYKSISEDLD RVTKEVLSSA AYIMGKNVTE FEKEFAEYIG VKHAISVGNG
TDALVIALKS LGIGHGDEVI TSTFTYFASA ECISAVGATP VFVDVEKDTF NIDPSKIEEK
ITDKTKAIIP VHIFGQSAEM DEINEIAKKH NLKVIEDACQ AVGAKYKGKM IGTLGDAACF
SFFPTKNLSC AGDGGMIVTD NDDIATIAKA LRTHGSGETG QKAYNLLNNI TEDIKTSKDG
DDTVYNPLKY YNYLIGFNSR LDAIQGAILR VKLPHLDSWN GKRREIAEIY NEKFKDADVV
TPINREENEV IYHQYVLQCD DRETMLNKLK EKGVATGVYY PVPLHLQKVY ADLGYKEGDM
PVAEYLSHRT FAIPVYPELT QEQIEYIVDA IK
//
