OTCC_MALP2
ID OTCC_MALP2 Reviewed; 342 AA.
AC Q8EVF5;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Ornithine carbamoyltransferase, catabolic {ECO:0000303|PubMed:23082227};
DE Short=OTCase {ECO:0000303|PubMed:23082227};
DE EC=2.1.3.3 {ECO:0000255|HAMAP-Rule:MF_01109};
GN Name=arcB; OrderedLocusNames=MYPE6090;
OS Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC Bacteria; Tenericutes; Mycoplasmoidales; Mycoplasmoidaceae; Malacoplasma.
OX NCBI_TaxID=272633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF-2;
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]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), FUNCTION, AND SUBUNIT.
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 -!- FUNCTION: nvolved in the catabolism of arginine. Catalyzes the
CC phosphorolysis of citrulline, the reverse reaction of the biosynthetic
CC one, yielding ornithine and carbamoyl phosphate which serve to generate
CC ATP from ADP. {ECO:0000305|PubMed:23082227}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline +
CC phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743,
CC ChEBI:CHEBI:58228; EC=2.1.3.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01109};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC pathway; carbamoyl phosphate from L-arginine: step 2/2.
CC {ECO:0000255|HAMAP-Rule:MF_01109}.
CC -!- SUBUNIT: Dodecamer (tetramer of trimers).
CC {ECO:0000269|PubMed:23082227}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01109}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000255|HAMAP-Rule:MF_01109}.
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DR EMBL; BA000026; BAC44399.1; -; Genomic_DNA.
DR RefSeq; WP_011077431.1; NC_004432.1.
DR PDB; 4AMU; X-ray; 2.50 A; A/B/C/D=1-342.
DR PDB; 4ANF; X-ray; 2.60 A; A/B/C/D=1-342.
DR PDBsum; 4AMU; -.
DR PDBsum; 4ANF; -.
DR AlphaFoldDB; Q8EVF5; -.
DR SMR; Q8EVF5; -.
DR STRING; 272633.26454069; -.
DR PRIDE; Q8EVF5; -.
DR EnsemblBacteria; BAC44399; BAC44399; BAC44399.
DR KEGG; mpe:MYPE6090; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_1_14; -.
DR OMA; DGNNVCN; -.
DR OrthoDB; 988597at2; -.
DR UniPathway; UPA00254; UER00365.
DR Proteomes; UP000002522; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019546; P:arginine deiminase pathway; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1370; -; 2.
DR HAMAP; MF_01109; OTCase; 1.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR InterPro; IPR002292; Orn/put_carbamltrans.
DR InterPro; IPR024904; OTCase_ArgI.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00102; OTCASE.
DR SUPFAM; SSF53671; SSF53671; 1.
DR TIGRFAMs; TIGR00658; orni_carb_tr; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Arginine metabolism; Cytoplasm; Reference proteome;
KW Transferase.
FT CHAIN 1..342
FT /note="Ornithine carbamoyltransferase, catabolic"
FT /id="PRO_0000112953"
FT BINDING 59..62
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 83
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 110
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 137..140
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 169
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 235
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 239..240
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 276..277
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 328
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:4AMU"
FT HELIX 18..36
FT /evidence="ECO:0007829|PDB:4AMU"
FT TURN 37..42
FT /evidence="ECO:0007829|PDB:4AMU"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:4AMU"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:4AMU"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:4AMU"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:4AMU"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:4AMU"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:4AMU"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:4AMU"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:4AMU"
FT HELIX 114..124
FT /evidence="ECO:0007829|PDB:4AMU"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:4AMU"
FT HELIX 138..152
FT /evidence="ECO:0007829|PDB:4AMU"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:4AMU"
FT HELIX 169..180
FT /evidence="ECO:0007829|PDB:4AMU"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:4AMU"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:4AMU"
FT HELIX 199..212
FT /evidence="ECO:0007829|PDB:4AMU"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:4AMU"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:4AMU"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:4AMU"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:4AMU"
FT HELIX 244..254
FT /evidence="ECO:0007829|PDB:4AMU"
FT HELIX 261..266
FT /evidence="ECO:0007829|PDB:4AMU"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:4AMU"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:4ANF"
FT HELIX 286..294
FT /evidence="ECO:0007829|PDB:4AMU"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:4AMU"
FT HELIX 300..304
FT /evidence="ECO:0007829|PDB:4AMU"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:4AMU"
FT HELIX 321..340
FT /evidence="ECO:0007829|PDB:4AMU"
SQ SEQUENCE 342 AA; 38036 MW; D21012AF209307A7 CRC64;
MPVNLKGRSL DSLLNFTTEE VQHLIDLSID LKKAKYQGLH INNRPLVGKN IAILFQKDST
RTRCAFEVAA SDLGAGVTYI GPSGSNMGKK ESIEDTAKVL GRFYDGIEFR GFAQSDVDAL
VKYSGVPVWN GLTDDEHPTQ IIADFMTMKE KFGNLKNKKI VFIGDYKNNV GVSTMIGAAF
NGMHVVMCGP DNYKNEIDKN VLAKCIELFK RNGGSLRFST DKILAAQDAD VIYTDVWVSL
GEPFELFDKR IGELKNFQVD MNMIKAAKND VIFLHCLPAF HDDHTSFSKE VATTLGAKYP
IVAKGEMEVT DEVFQSLHNK AFDQAENRMH SIKAIILSTI GY
