ID C7MN79_CRYCD Unreviewed; 331 AA.
AC C7MN79;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 13-SEP-2023, entry version 84.
DE RecName: Full=Ornithine carbamoyltransferase, catabolic {ECO:0000256|HAMAP-Rule:MF_01109};
DE Short=OTCase {ECO:0000256|HAMAP-Rule:MF_01109};
DE EC=2.1.3.3 {ECO:0000256|HAMAP-Rule:MF_01109};
GN Name=arcB {ECO:0000256|HAMAP-Rule:MF_01109};
GN OrderedLocusNames=Ccur_06550 {ECO:0000313|EMBL:ACU94369.1};
OS Cryptobacterium curtum (strain ATCC 700683 / DSM 15641 / CCUG 43107 /
OS 12-3).
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Cryptobacterium.
OX NCBI_TaxID=469378 {ECO:0000313|EMBL:ACU94369.1, ECO:0000313|Proteomes:UP000000954};
RN [1] {ECO:0000313|EMBL:ACU94369.1, ECO:0000313|Proteomes:UP000000954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700683 / DSM 15641 / 12-3
RC {ECO:0000313|Proteomes:UP000000954};
RX PubMed=21304644; DOI=10.40456/sigs.12260;
RA Mavrommatis K., Pukall R., Rohde C., Chen F., Sims D., Brettin T.,
RA Kuske C., Detter J.C., Han C., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Nolan M., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA Ovchinnikova G., Pati A., Ivanova N., Chen A., Palaniappan K., Chain P.,
RA D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Rohde M., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Cryptobacterium curtum type strain (12-3).";
RL Stand. Genomic Sci. 1:93-100(2009).
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;
CC Evidence={ECO:0000256|ARBA:ARBA00001065, ECO:0000256|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:0000256|HAMAP-Rule:MF_01109}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000256|ARBA:ARBA00007805,
CC ECO:0000256|HAMAP-Rule:MF_01109}.
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DR EMBL; CP001682; ACU94369.1; -; Genomic_DNA.
DR RefSeq; WP_012803057.1; NC_013170.1.
DR AlphaFoldDB; C7MN79; -.
DR STRING; 469378.Ccur_06550; -.
DR KEGG; ccu:Ccur_06550; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_1_11; -.
DR OMA; VATDVWV; -.
DR OrthoDB; 9802587at2; -.
DR UniPathway; UPA00254; UER00365.
DR Proteomes; UP000000954; 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; Aspartate/ornithine carbamoyltransferase; 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 NCBIfam; TIGR00658; orni_carb_tr; 1.
DR PANTHER; PTHR45753:SF2; ORNITHINE CARBAMOYLTRANSFERASE; 1.
DR PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00102; OTCASE.
DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 3: Inferred from homology;
KW Arginine metabolism {ECO:0000256|HAMAP-Rule:MF_01109};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109};
KW Reference proteome {ECO:0000313|Proteomes:UP000000954};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01109}.
FT DOMAIN 8..148
FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02729"
FT DOMAIN 156..328
FT /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00185"
FT BINDING 57..60
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 84
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 108
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 135..138
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 168
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 232
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 236..237
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 273..274
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 318
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
SQ SEQUENCE 331 AA; 36766 MW; 4FA66229CD843034 CRC64;
MPTSLSGRDF LKLLDFSTSE IKYLLKLSRE FKNLKLTGTP HRYLEGKNIV LLFQKTSTRT
RCAFEVGALD LGMGVTYLDP GSSQMGKKES IEDTARVLER FYDGIEFRGF AQKDVQDLAD
NATVPVWNGL TTEWHPTQML ADILTIQEEF GDDIAGRTLV FMGDAKNNVA RSLMVVCAKL
GLNFVACGPK DCMPGDDVVE ACKPIAADNG CTIKLTSDVR EGVTGADVIY TDVWVSMGEP
DEVWASRIKE LEAYRVTRDV MALAKPEAIF LHCLPAFHDT NTTIGAEKAK QFGITEMEVT
DEVFEGKQSR VFDEAENRMH TIKAVMYATL S
//