Reviewed, UniProtKB/Swiss-Prot Q8GG79 (OTCC_STRSU)

Names and origin

Protein names

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

Gene names

Name:	arcB
ORF Names:	SsuiDRAFT_2842

Organism

Streptococcus suis

Taxonomic identifier

1307 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	337 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Carbamoyl phosphate + L-ornithine = phosphate + L-citrulline. HAMAP MF_01109
Pathway	Amino-acid degradation; L-arginine degradation via ADI pathway; carbamoyl phosphate from L-arginine: step 2/2. HAMAP MF_01109
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the ATCase/OTCase family.

Ontologies

Keywords
Biological process	Arginine metabolism
Cellular component	Cytoplasm
Molecular function	Transferase
Gene Ontology (GO)
Biological process	arginine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	ornithine carbamoyltransferase complex Inferred from electronic annotation. Source: InterPro
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 – 337	337	Ornithine carbamoyltransferase, catabolic HAMAP MF_01109		PRO_0000113043
Regions
	Region	57 – 61	5	Carbamoyl phosphate binding By similarity
	Region	271 – 274	4	Ornithine binding By similarity
Sites
	Binding site	108	1	Carbamoyl phosphate By similarity
	Binding site	135	1	Carbamoyl phosphate By similarity
	Site	32	1	Important for structural integrity By similarity
	Site	148	1	Important for structural integrity By similarity
Experimental info
	Sequence conflict	203	1	G → V in EEF64413. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q8GG79-1 [UniParc]. Last modified May 30, 2006. Version 2. Checksum: C5E42EFCAFC3EC47	FASTA	337	37,856
	10 20 30 40 50 60 MTNVFKGRHF LAEKDFTRAE LEWLIDFSAH LKDLKKRNIP HRYLEGKNIA LLFEKTSTRT 70 80 90 100 110 120 RAAFTVASID LGAHPEYLGA NDIQLGKKES TEDTAKVLGR MFDGIEFRGF SQKMVEELAE 130 140 150 160 170 180 FSGVPVWNGL TDAWHPTQML ADYLTVKENF GKLEGLTLVY CGDGRNNVAN SLLVTGAILG 190 200 210 220 230 240 VNVHIFSPKE LFPEEEVVAL AEGFAKESGA RVLITDNADE AVKGADVLYT DVWVSMGEED 250 260 270 280 290 300 KFAERVALLK PYQVNMELVK KAENENLIFL HCLPAFHDTN TVYGKDVAEK FGVEEMEVTD 310 320 330 EVFRSKYARH FDQAENRMHT IKAVMAATLG DPFVPRV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of two temperature-induced surface-associated proteins of Streptococcus suis with high homologies to members of the arginine deiminase system of Streptococcus pyogenes." Winterhoff N., Goethe R., Gruening P., Valentin-Weigand P. J. Bacteriol. 184:6768-6776(2002) [PubMed: 12446626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: I9841/1.
[2]	Gruening P., Fulde M., Goethe R., Valentin-Weigand P., Winterhoff N. Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 163; 187 AND 292.
[3]	"Sequencing of the draft genome and assembly of Streptococcus suis 89/1591." US DOE Joint Genome Institute (JGI-PGF) Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Chertkov O., Brettin T., Han C., Detter J.C., Gottschalk M., Richardson P. Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 89/1591.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF546864 Genomic DNA. Translation: AAN76308.2. AAFA03000016 Genomic DNA. Translation: EEF64413.1.
3D structure databases
HSSP	HSSP built from PDB template 1AKM based on UniProtKB P04391.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.1.3.3. 275564.
Family and domain databases
HAMAP	MF_01109. [Tree]
InterPro	IPR006132. Asp/Orn_carbamoyltranf_P_bd. IPR006130. Asp/Orn_carbamoylTrfase. IPR006131. Asp_carbamoyltransf_Asp/Orn_bd. IPR002292. Orn_carbamltrans. [Graphical view]
Pfam	PF00185. OTCace. 1 hit. PF02729. OTCace_N. 1 hit. [Graphical view]
PRINTS	PR00100. AOTCASE. PR00102. OTCASE.
TIGRFAMs	TIGR00658. orni_carb_tr. 1 hit.
PROSITE	PS00097. CARBAMOYLTRANSFERASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

OTCC_STRSU

Accession

Primary (citable) accession number: Q8GG79
Secondary accession number(s): B9WVS9, Q301C2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2003
Last sequence update:	May 30, 2006
Last modified:	October 13, 2009
This is version 37 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)