Q48296 (OTCC_HALSA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ornithine carbamoyltransferase, catabolic
Short name=cOTCase
EC=2.1.3.3

Gene names

Name:	arcB
Synonyms:	argB
Ordered Locus Names:	VNG_6315G

Encoded on

Plasmid pNRC200 Ref.3

Organism

Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium) [Reference proteome] [HAMAP]

Taxonomic identifier

64091 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Halobacterium › Halobacterium salinarum

Protein attributes

Sequence length	295 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. Ref.1
Catalytic activity	Carbamoyl phosphate + L-ornithine = phosphate + L-citrulline. HAMAP-Rule MF_01109
Enzyme regulation	Arginine lead to a slight activation. Inhibited by all nucleotide phosphates. Ref.1
Pathway	Amino-acid degradation; L-arginine degradation via ADI pathway; carbamoyl phosphate from L-arginine: step 2/2. HAMAP-Rule MF_01109
Subunit structure	Homohexamer. Ref.1
Subcellular location	Cytoplasm Probable HAMAP-Rule MF_01109.
Miscellaneous	Not stable below 1 M KCl (Ref.1). HAMAP-Rule MF_01109
Sequence similarities	Belongs to the ATCase/OTCase family.
Biophysicochemical properties	Kinetic parameters: KM=0.4 mM for carbamoyl phosphate Ref.1 KM=8 mM for L-ornithine pH dependence: Optimum pH is 8.8. At the physiological pH of 7, activity is only about 30%.

Ontologies

Keywords
Biological process	Arginine metabolism
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	Complete proteome Direct protein sequencing Plasmid Reference proteome
Gene Ontology (GO)
Biological_process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP arginine catabolic process to ornithine Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	amino acid binding Inferred from electronic annotation. Source: InterPro ornithine carbamoyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 295	295	Ornithine carbamoyltransferase, catabolic HAMAP-Rule MF_01109		PRO_0000113063
Regions
	Region	49 – 53	5	Carbamoyl phosphate binding By similarity
	Region	127 – 130	4	Carbamoyl phosphate binding By similarity
	Region	217 – 218	2	Ornithine binding By similarity
	Region	252 – 255	4	Carbamoyl phosphate binding By similarity
Sites
	Binding site	5	1	Carbamoyl phosphate By similarity
	Binding site	65	1	Carbamoyl phosphate By similarity
	Binding site	76	1	Carbamoyl phosphate By similarity
	Binding site	100	1	Carbamoyl phosphate By similarity
	Binding site	155	1	Ornithine By similarity
	Binding site	213	1	Ornithine By similarity
	Binding site	263	1	Carbamoyl phosphate By similarity
	Binding site	281	1	Carbamoyl phosphate By similarity
	Site	26	1	Important for structural integrity By similarity
	Site	140	1	Important for structural integrity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q48296 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: BFF6E002AC0289A2	FASTA	295	32,676
	10 20 30 40 50 60 MEHLVDINDV ESEEIEQLLD LAASMKENPG EFSGVMDNKS LVMLFAKPST RTRLSFETGM 70 80 90 100 110 120 TQLGGHGIFF EMGSSQLSRG EPISDVSQVM SRYEDAIMAR LFEHDEMMEL AENADVPVVN 130 140 150 160 170 180 GLTDFLHPCQ ALTDMFTMQE KDRLDTLAFV GDGNNVAHSL MQASAKMGVD CRIATPEGME 190 200 210 220 230 240 PDEEIQDRVS DANVTVTNDP YEAVDGATAV YGDVFVSMGE EEQREEKLAE FDGFQIDQDL 250 260 270 280 290 MDAARDDAIF MHCLPAHRGE EVTAEVADGP QSVIFDQAEN RMHVQKAIVH TLVNQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Catabolic ornithine transcarbamylase of Halobacterium halobium (salinarium): purification, characterization, sequence determination, and evolution." Ruepp A., Mueller H., Lottspeich F., Soppa J. J. Bacteriol. 177:1129-1136(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION AS A COTCASE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT. Strain: L33.
[2]	"Fermentative arginine degradation in Halobacterium salinarium (formerly Halobacterium halobium): genes, gene products, and transcripts of the arcRACB gene cluster." Ruepp A., Soppa J. J. Bacteriol. 178:4942-4947(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: L33.
[3]	"Genome sequence of Halobacterium species NRC-1." Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D., Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D., Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K. , Cruz R., Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P., Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M., Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J., Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L., DasSarma S. Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700922 / JCM 11081 / NRC-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X81712 Genomic DNA. Translation: CAA57356.1. X80931 Genomic DNA. Translation: CAA56906.1. AE004438 Genomic DNA. Translation: AAG20946.1.
PIR	S49261.
RefSeq	NP_395811.1. NC_002608.1.
3D structure databases
ProteinModelPortal	Q48296.
ModBase	Search...
Protein-protein interaction databases
STRING	64091.VNG6315G.
Proteomic databases
PaxDb	Q48296.
PRIDE	Q48296.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAG20946; AAG20946; VNG_6315G.
GeneID	1449194.
KEGG	hal:VNG6315G.
Phylogenomic databases
eggNOG	COG0078.
KO	K00611.
OMA	AHPCQTL.
ProtClustDB	PRK00779.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-662.
UniPathway	UPA00254; UER00365.
Family and domain databases
HAMAP	MF_01109. OTCase.
InterPro	IPR006132. Asp/Orn_carbamoyltranf_P-bd. IPR006130. Asp/Orn_carbamoylTrfase. IPR006131. Asp_carbamoyltransf_Asp/Orn-bd. IPR002292. Orn/put_carbamltrans. IPR024904. Orn_carbamltrans. [Graphical view]
Pfam	PF00185. OTCace. 1 hit. PF02729. OTCace_N. 1 hit. [Graphical view]
PRINTS	PR00100. AOTCASE. PR00102. OTCASE.
SUPFAM	SSF53671. Asp/Orn_carbamoyltranf. 1 hit.
TIGRFAMs	TIGR00658. orni_carb_tr. 1 hit.
PROSITE	PS00097. CARBAMOYLTRANSFERASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

OTCC_HALSA

Accession

Primary (citable) accession number: Q48296
Secondary accession number(s): Q59454, Q9HHN0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program