Reviewed, UniProtKB/Swiss-Prot Q9K451 (COX1B_STRCO)

Names and origin

Protein names

Recommended name:
    Putative cytochrome c oxidase subunit 1-beta
    EC=1.9.3.1
Alternative name(s):
    Cytochrome c oxidase polypeptide I-beta
    Cytochrome aa3 subunit 1-beta

Gene names

Name:	ctaD2
Ordered Locus Names:	SCO7234
ORF Names:	SC2H12.33

Organism

Streptomyces coelicolor [Complete proteome] [HAMAP]

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	573 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B By similarity.
Catalytic activity	4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.
Cofactor	Binds 1 copper B per subunit By similarity. Binds 2 heme groups per subunit By similarity.
Pathway	Energy metabolism; oxidative phosphorylation.
Subunit structure	Associates with subunits II, III and IV to form cytochrome c oxidase By similarity.
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the heme-copper respiratory oxidase family.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Ligand	Copper Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	aerobic respiration Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW cytochrome-c oxidase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 573	573	Putative cytochrome c oxidase subunit 1-beta		PRO_0000183453
Regions
	Transmembrane	53 – 73	21	Potential
	Transmembrane	103 – 123	21	Potential
	Transmembrane	141 – 161	21	Potential
	Transmembrane	188 – 208	21	Potential
	Transmembrane	227 – 247	21	Potential
	Transmembrane	272 – 292	21	Potential
	Transmembrane	304 – 324	21	Potential
	Transmembrane	329 – 349	21	Potential
	Transmembrane	373 – 393	21	Potential
	Transmembrane	412 – 432	21	Potential
	Transmembrane	447 – 467	21	Potential
	Transmembrane	490 – 510	21	Potential
Sites
	Metal binding	100	1	Iron (heme A axial ligand) By similarity
	Metal binding	278	1	Copper B By similarity
	Metal binding	282	1	Copper B By similarity
	Metal binding	327	1	Copper B By similarity
	Metal binding	328	1	Copper B By similarity
	Metal binding	411	1	Iron (heme A3 axial ligand) By similarity
	Metal binding	413	1	Iron (heme A axial ligand) By similarity
Amino acid modifications
	Cross-link	278 ↔ 282		1'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9K451-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 1FC5DC79FD6DA220	FASTA	573	64,041
	10 20 30 40 50 60 MVVGLSPRRL GTLRRMAVDR RTKSPRRTPA RQRTNRTLGR ALVRWATTTD HKVIGHLYLA 70 80 90 100 110 120 TSFGFFLLGG VLAMLMRSEL ARPGLQLFSN EQYNQLFTVH GTIMMLLFAT PLFAGFTNVI 130 140 150 160 170 180 MPLQIGAPDL AFPRLNALSY WMYLFGGLMV VSGFLTPGGA ASFGWFAYAP LNSATFSPGP 190 200 210 220 230 240 GGDLWTMGLV VSGVSTTLSA VNFISTIICL RAPGMTMFRM PIFTWNILFT SILVLPAFPV 250 260 270 280 290 300 LTAALLMLEA DRKFGAHVFD AANGGALLWQ HLFWFFGHPE VYIVALPFFG IVTEIIPVFS 310 320 330 340 350 360 RKPIFGYVSL VGATIAITFL SAVVWAHHMF ATGAVLLPFF SLMSFLIAVP TGVKFFNWIG 370 380 390 400 410 420 TMIRGSLSFE TPMLWACGFL VTFLLGGMSG VLIASPPLDF HLTDSYFIVA HLHYVLFGTV 430 440 450 460 470 480 VFAMFAGFYF WWPKFTGKLL DERLGKIHFW TLFVGFQTTF LVQHWLGEQG MPRRYADYLA 490 500 510 520 530 540 ADGFTTLNTI SSIGAFLLGL STLPFLYNVW RTHQYGEKVG RDDPWGYGRS LEWATSSPPP 550 560 570 RHNFTSLPRI RSESPAFDLH HPDVTRHDQR HVQ

References

[1]

"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed: 12000953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL939130 Genomic DNA. Translation: CAB94657.1.
RefSeq	NP_631290.1.
3D structure databases
HSSP	HSSP built from PDB template 1FFT based on UniProtKB P18401.
ModBase	Search...
Genome annotation databases
GeneID	1102672.
GenomeReviews	Gene locus SCO7234 in contig AL645882_GR.
KEGG	sco:SCO7234.
NMPDR	fig|100226.1.peg.7168.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9K451.
OMA	Q9K451. NTISSIG.
Enzyme and pathway databases
BioCyc	SCOE100226:SCO7234-MON.
BRENDA	1.9.3.1. 1084.
Family and domain databases
InterPro	IPR000883. Cyt_c_oxidase_su1. IPR014241. Cyt_c_oxidase_su1_bac. [Graphical view]
Gene3D	G3DSA:1.20.210.10. COX1. 1 hit.
PANTHER	PTHR10422. COX1. 1 hit.
Pfam	PF00115. COX1. 1 hit. [Graphical view]
PRINTS	PR01165. CYCOXIDASEI.
TIGRFAMs	TIGR02891. CtaD_CoxA. 1 hit.
PROSITE	PS50855. COX1. 1 hit. PS00077. COX1_CUB. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

COX1B_STRCO

Accession

Primary (citable) accession number: Q9K451

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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