PYRI_METHJ
ID PYRI_METHJ Reviewed; 155 AA.
AC Q2FN10;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Aspartate carbamoyltransferase regulatory chain {ECO:0000255|HAMAP-Rule:MF_00002};
GN Name=pyrI {ECO:0000255|HAMAP-Rule:MF_00002}; OrderedLocusNames=Mhun_0619;
OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS JF-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=323259;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL Stand. Genomic Sci. 11:2-2(2016).
CC -!- FUNCTION: Involved in allosteric regulation of aspartate
CC carbamoyltransferase. {ECO:0000255|HAMAP-Rule:MF_00002}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00002};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00002};
CC -!- SUBUNIT: Contains catalytic and regulatory chains. {ECO:0000255|HAMAP-
CC Rule:MF_00002}.
CC -!- SIMILARITY: Belongs to the PyrI family. {ECO:0000255|HAMAP-
CC Rule:MF_00002}.
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DR EMBL; CP000254; ABD40375.1; -; Genomic_DNA.
DR RefSeq; WP_011447660.1; NC_007796.1.
DR AlphaFoldDB; Q2FN10; -.
DR SMR; Q2FN10; -.
DR STRING; 323259.Mhun_0619; -.
DR EnsemblBacteria; ABD40375; ABD40375; Mhun_0619.
DR GeneID; 3922566; -.
DR KEGG; mhu:Mhun_0619; -.
DR eggNOG; arCOG04229; Archaea.
DR HOGENOM; CLU_128576_0_0_2; -.
DR OMA; CPNRNCI; -.
DR OrthoDB; 101957at2157; -.
DR Proteomes; UP000001941; Chromosome.
DR GO; GO:0009347; C:aspartate carbamoyltransferase complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.140; -; 1.
DR HAMAP; MF_00002; Asp_carb_tr_reg; 1.
DR InterPro; IPR020545; Asp_carbamoyltransf_reg_N.
DR InterPro; IPR002801; Asp_carbamoylTrfase_reg.
DR InterPro; IPR020542; Asp_carbamoyltrfase_reg_C.
DR InterPro; IPR036792; Asp_carbatrfase_reg_C_sf.
DR InterPro; IPR036793; Asp_carbatrfase_reg_N_sf.
DR PANTHER; PTHR35805; PTHR35805; 1.
DR Pfam; PF01948; PyrI; 1.
DR Pfam; PF02748; PyrI_C; 1.
DR SUPFAM; SSF54893; SSF54893; 1.
DR SUPFAM; SSF57825; SSF57825; 1.
DR TIGRFAMs; TIGR00240; ATCase_reg; 1.
PE 3: Inferred from homology;
KW Metal-binding; Pyrimidine biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..155
FT /note="Aspartate carbamoyltransferase regulatory chain"
FT /id="PRO_0000321507"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00002"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00002"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00002"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00002"
SQ SEQUENCE 155 AA; 16965 MW; 840AE907036D69FE CRC64;
MTNEEPKRTL VISTIENGTV IDHIKAGEAL TVLRILGITG STRECVSVAT NVSSKAQEKK
DVVKIEKREL KAQEVDRIAL VAPNATINII RNFRVIEKKG VIIPPVLIGV LRCPNPCCIT
NTNEPVMSRF EMHGKKAVCS YCDAVISSDI SSHII
