OTCC_LENHI
ID OTCC_LENHI Reviewed; 343 AA.
AC Q8G998;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Ornithine carbamoyltransferase, catabolic {ECO:0000303|PubMed:19666033};
DE Short=OTCase {ECO:0000303|PubMed:19666033};
DE EC=2.1.3.3 {ECO:0000255|HAMAP-Rule:MF_01109};
GN Name=arcB {ECO:0000303|PubMed:12490324};
OS Lentilactobacillus hilgardii (Lactobacillus hilgardii).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1588;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=X(1)B;
RX PubMed=12490324; DOI=10.1016/s0378-1119(02)01083-1;
RA Arena M.E., Manca de Nadra M.C., Munoz R.;
RT "The arginine deiminase pathway in the wine lactic acid bacterium
RT Lactobacillus hilgardii X1B: structural and functional study of the arcABC
RT genes.";
RL Gene 301:61-66(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NICKEL ION, FUNCTION
RP AS AN OTCASE, MUTAGENESIS OF 337-ASN--VAL-343, AND SUBUNIT.
RX PubMed=19666033; DOI=10.1016/j.jmb.2009.08.002;
RA de Las Rivas B., Fox G.C., Angulo I., Ripoll M.M., Rodriguez H., Munoz R.,
RA Mancheno J.M.;
RT "Crystal structure of the hexameric catabolic ornithine transcarbamylase
RT from Lactobacillus hilgardii: Structural insights into the oligomeric
RT assembly and metal binding.";
RL J. Mol. Biol. 393:425-434(2009).
CC -!- FUNCTION: Involved 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:19666033}.
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 -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:19666033};
CC Note=Ni(2+) ion bind each monomer of the trimer.
CC {ECO:0000269|PubMed:19666033};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC pathway; carbamoyl phosphate from L-arginine: step 2/2.
CC {ECO:0000305|PubMed:19666033}.
CC -!- SUBUNIT: Homohexamer; dimer of trimers. {ECO:0000269|PubMed:19666033}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01109}.
CC -!- MISCELLANEOUS: The C-terminal end of the protein is critical for the
CC stabilization of this oligomer. {ECO:0000269|PubMed:19666033}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000255|HAMAP-Rule:MF_01109}.
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DR EMBL; AJ421514; CAD13392.1; -; Genomic_DNA.
DR RefSeq; WP_003552004.1; NZ_PUFR01000061.1.
DR PDB; 2W37; X-ray; 2.10 A; A/B/C=1-343.
DR PDBsum; 2W37; -.
DR AlphaFoldDB; Q8G998; -.
DR SMR; Q8G998; -.
DR BRENDA; 2.1.3.3; 2871.
DR UniPathway; UPA00254; UER00365.
DR EvolutionaryTrace; Q8G998; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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; Metal-binding; Nickel;
KW Transferase.
FT CHAIN 1..343
FT /note="Ornithine carbamoyltransferase, catabolic"
FT /id="PRO_0000112932"
FT BINDING 62..65
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P04391"
FT BINDING 79
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000269|PubMed:19666033"
FT BINDING 89
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P04391"
FT BINDING 113
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P04391"
FT BINDING 140..143
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P04391"
FT BINDING 172
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P04391"
FT BINDING 236
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P04391"
FT BINDING 240..241
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P04391"
FT BINDING 278..279
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P04391"
FT BINDING 323
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P04391"
FT MUTAGEN 337..343
FT /note="Missing: It generates a metastable mutant that
FT behaves as a mixture of monomeric and trimeric species with
FT only the latter exhibiting OTC activity."
FT /evidence="ECO:0000269|PubMed:19666033"
FT TURN 9..12
FT /evidence="ECO:0007829|PDB:2W37"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:2W37"
FT HELIX 23..42
FT /evidence="ECO:0007829|PDB:2W37"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:2W37"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:2W37"
FT HELIX 63..75
FT /evidence="ECO:0007829|PDB:2W37"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:2W37"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:2W37"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:2W37"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:2W37"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:2W37"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:2W37"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:2W37"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:2W37"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:2W37"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:2W37"
FT HELIX 172..184
FT /evidence="ECO:0007829|PDB:2W37"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:2W37"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:2W37"
FT HELIX 200..213
FT /evidence="ECO:0007829|PDB:2W37"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:2W37"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:2W37"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:2W37"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:2W37"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:2W37"
FT HELIX 260..264
FT /evidence="ECO:0007829|PDB:2W37"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:2W37"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:2W37"
FT HELIX 288..297
FT /evidence="ECO:0007829|PDB:2W37"
FT HELIX 306..309
FT /evidence="ECO:0007829|PDB:2W37"
FT HELIX 316..335
FT /evidence="ECO:0007829|PDB:2W37"
SQ SEQUENCE 343 AA; 38280 MW; FF7158C4581F684B CRC64;
MTKDFRQNVF QGRSVLAEKD FSAAELEYLI DFGLHLKALK KAGIPHHYLE GKNIALLFEK
SSTRTRSAFT TASIDLGAHP EYLGQNDIQL GKKESTSDTA KVLGSMFDGI EFRGFKQSDA
EILARDSGVP VWNGLTDEWH PTQMLADFMT VKENFGKLQG LTLTFMGDGR NNVANSLLVT
GAILGVNIHI VAPKALFPTE ETQNIAKGFA EKSGAKLVIT DDLDEGLKGS NVVYTDVWVS
MGESNWEERV KELTPYQVNM EAMKKTGTPD DQLIFMHCLP AFHNTDTQYG KEIKEKYGIT
EMEVTDEVFT SKYARQFEEA ENRMHSIKAM MAATLGNLFI PRV
