ID D1B9C4_THEAS Unreviewed; 411 AA.
AC D1B9C4;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:ACZ18877.1};
GN OrderedLocusNames=Taci_0641 {ECO:0000313|EMBL:ACZ18877.1};
OS Thermanaerovibrio acidaminovorans (strain ATCC 49978 / DSM 6589 / Su883)
OS (Selenomonas acidaminovorans).
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Thermanaerovibrio.
OX NCBI_TaxID=525903 {ECO:0000313|EMBL:ACZ18877.1, ECO:0000313|Proteomes:UP000002030};
RN [1] {ECO:0000313|EMBL:ACZ18877.1, ECO:0000313|Proteomes:UP000002030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49978 / DSM 6589 / Su883
RC {ECO:0000313|Proteomes:UP000002030};
RX PubMed=21304665; DOI=10.4056/sigs.40645;
RA Chovatia M., Sikorski J., Schroder M., Lapidus A., Nolan M., Tice H.,
RA Glavina Del Rio T., Copeland A., Cheng J.F., Lucas S., Chen F., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Chain P., Saunders E., Detter J.C., Brettin T., Rohde M.,
RA Goker M., Spring S., Bristow J., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Eisen J.A.;
RT "Complete genome sequence of Thermanaerovibrio acidaminovorans type strain
RT (Su883).";
RL Stand. Genomic Sci. 1:254-261(2009).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; CP001818; ACZ18877.1; -; Genomic_DNA.
DR RefSeq; WP_012869393.1; NC_013522.1.
DR RefSeq; YP_003317159.1; NC_013522.1.
DR AlphaFoldDB; D1B9C4; -.
DR STRING; 525903.Taci_0641; -.
DR EnsemblBacteria; ACZ18877; ACZ18877; Taci_0641.
DR KEGG; tai:Taci_0641; -.
DR PATRIC; fig|525903.6.peg.647; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_2_2_0; -.
DR OrthoDB; 9761532at2; -.
DR Proteomes; UP000002030; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF3; ACETYLORNITHINE DEACETYLASE-RELATED; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002030}.
FT DOMAIN 205..313
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 411 AA; 44466 MW; 11AAC36247C5BA0C CRC64;
MSRFCGDPLD DKVLAYEGAM VEALCGLVRR PAISPDDGGL GEYDKALYIE SLVSSLGLGP
VEMYGSPDPR AKGGVRPNLV LRVPGSYRDL PRLWIFTHMD VVPEGDRGLW ESDPFEPVVR
DGMVIGRGAN DNGQELVASL FALKAVVDQG GPGREVCLAF VADEEVGSEH GIGFLMREHR
DLFSPSDLVL VPDGGNEAGD FIEVAEKTIL WVEFQVLGRQ VHASRPDQGI NACRVANELS
VNLDRALRSA FPESDPLFEP AISTFEPTRR LQNVANVNTV PGREVFALDC RVLPHVPVSE
VEKVIAAEVR KVEDAYGAKV SHRFLQKGDP TPVTDPASPV VELLTRSVQS VLGVSPRVGG
IGGGTCAAFF RANGIPAAVW AQETDTAHMP GEYALVEHML NEARVFARMF A
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