ID   Q8EVF4_MALP2            Unreviewed;       309 AA.
AC   Q8EVF4;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=Carbamate kinase {ECO:0000256|PIRNR:PIRNR000723};
GN   OrderedLocusNames=MYPE6100 {ECO:0000313|EMBL:BAC44400.1};
OS   Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Malacoplasma.
OX   NCBI_TaxID=272633 {ECO:0000313|EMBL:BAC44400.1, ECO:0000313|Proteomes:UP000002522};
RN   [1] {ECO:0000313|EMBL:BAC44400.1, ECO:0000313|Proteomes:UP000002522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HF-2 {ECO:0000313|EMBL:BAC44400.1,
RC   ECO:0000313|Proteomes:UP000002522};
RX   PubMed=12466555; DOI=10.1093/nar/gkf667;
RA   Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA   Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT   "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT   bacterial pathogen in humans.";
RL   Nucleic Acids Res. 30:5293-5300(2002).
RN   [2] {ECO:0007829|PDB:4AXS}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
RX   PubMed=23082227; DOI=10.1371/journal.pone.0047886;
RA   Gallego P., Planell R., Benach J., Querol E., Perez-Pons J.A., Reverter D.;
RT   "Structural characterization of the enzymes composing the arginine
RT   deiminase pathway in Mycoplasma penetrans.";
RL   PLoS ONE 7:E47886-E47886(2012).
CC   -!- SIMILARITY: Belongs to the carbamate kinase family.
CC       {ECO:0000256|ARBA:ARBA00011066, ECO:0000256|PIRNR:PIRNR000723}.
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DR   EMBL; BA000026; BAC44400.1; -; Genomic_DNA.
DR   RefSeq; WP_011077432.1; NC_004432.1.
DR   PDB; 4AXS; X-ray; 2.50 A; A=1-309.
DR   PDBsum; 4AXS; -.
DR   AlphaFoldDB; Q8EVF4; -.
DR   SMR; Q8EVF4; -.
DR   STRING; 272633.gene:10731727; -.
DR   KEGG; mpe:MYPE6100; -.
DR   eggNOG; COG0549; Bacteria.
DR   HOGENOM; CLU_076278_0_0_14; -.
DR   InParanoid; Q8EVF4; -.
DR   Proteomes; UP000002522; Chromosome.
DR   GO; GO:0008804; F:carbamate kinase activity; IEA:InterPro.
DR   GO; GO:0006525; P:arginine metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd04235; AAK_CK; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR003964; Carb_kinase.
DR   PANTHER; PTHR30409; CARBAMATE KINASE; 1.
DR   PANTHER; PTHR30409:SF1; CARBAMATE KINASE-RELATED; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF000723; Carbamate_kin; 1.
DR   PRINTS; PR01469; CARBMTKINASE.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4AXS};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002522};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000723}.
FT   DOMAIN          3..282
FT                   /note="Aspartate/glutamate/uridylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00696"
SQ   SEQUENCE   309 AA;  32749 MW;  F07B24BDB4CE3025 CRC64;
     MSRIVIALGG NALGDNPSQQ KELVKIPAAK IAALIQEGHE VIVGHGNGPQ VGMIFNAFAD
     AKKANEKTAL VPFAEAGGMS QGYIGYHMLT AISNELKKLN IQKDVLYFLT QTIVDANDPA
     FKNPTKPVGP FYSSKEIAEA NNPNSVIVED AGRGFRKVVA SPIPVDFIGI DAIKQNVNNG
     CVCIVGGGGG IPTIIQDNQY IGVDGVIDKD FALAKIADAV NADIFVVLTA VDYVYVDFNK
     PTQKALKTVD VKALNNFINQ DQFAKGSMLP KIKAAMGFVN GHPNRSAIIA DLSKVEDALK
     GLSGTKIIA
//