Reviewed, UniProtKB/Swiss-Prot Q9X813 (COX1A_STRCO)

Names and origin

Protein names

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

Gene names

Name:	ctaD1
Ordered Locus Names:	SCO2155
ORF Names:	SC6G10.28c

Organism

Streptomyces coelicolor [Complete proteome] [HAMAP]

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	578 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-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW 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 – 578	578	Probable cytochrome c oxidase subunit 1-alpha		PRO_0000183452
Regions
	Transmembrane	44 – 64	21	Potential
	Transmembrane	93 – 113	21	Potential
	Transmembrane	125 – 145	21	Potential
	Transmembrane	174 – 194	21	Potential
	Transmembrane	217 – 237	21	Potential
	Transmembrane	262 – 282	21	Potential
	Transmembrane	294 – 314	21	Potential
	Transmembrane	319 – 339	21	Potential
	Transmembrane	363 – 383	21	Potential
	Transmembrane	402 – 422	21	Potential
	Transmembrane	437 – 457	21	Potential
	Transmembrane	480 – 500	21	Potential
Sites
	Metal binding	90	1	Iron (heme A axial ligand) By similarity
	Metal binding	268	1	Copper B By similarity
	Metal binding	272	1	Copper B By similarity
	Metal binding	317	1	Copper B By similarity
	Metal binding	318	1	Copper B By similarity
	Metal binding	401	1	Iron (heme A3 axial ligand) By similarity
	Metal binding	403	1	Iron (heme A axial ligand) By similarity
Amino acid modifications
	Cross-link	268 ↔ 272		1'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9X813-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 2A25FF2A913DC461	FASTA	578	64,122
	10 20 30 40 50 60 MSILNEPQGA SAAEDSYENE LPVRRKQPGN VVIKWLTTTD HKTIGTMYLV TSFAFFVIGG 70 80 90 100 110 120 VMALFMRAEL ARPGLQIMSN EQFNQAFTMH GTIMLLMFAT PLFAGFANWI MPLQIGAPDV 130 140 150 160 170 180 AFPRLNMFAY WLYLFGSTIA VGGFLTPQGA ADFGWFAYSP LSDAVHSPGI GGDLWIMGLA 190 200 210 220 230 240 FSGFGTILGS VNFITTIICM RAPGMTMFRM PIFTWNVLLT GVLVLLAFPV LAAALFALEA 250 260 270 280 290 300 DRKFGAHIFD SSNGGALLWQ HLFWFFGHPE VYIIALPFFG IVSEIIPVFS RKPIFGYMGL 310 320 330 340 350 360 IGATIAIAGL SVTVWAHHMY VTGGVLLPFF SFMTFLIAVP TGVKFFNWIG TMWKGSLSFE 370 380 390 400 410 420 TPMLWSTGFL ITFLFGGLTG VILASPPLDF HVSDSYFVVA HFHYVVFGTV VFAMFAGFHF 430 440 450 460 470 480 WWPKFTGKML DERLGKITFW TLFVGFHGTF LVQHWLGAEG MPRRYADYLA ADGFTALNTI 490 500 510 520 530 540 STISSFLLGM SILPFFYNIW KTAKYGKKIE VDDPWGYGRS LEWATSCPPP RHNFLTLPRI 550 560 570 RSESPAFDLH HPEISAIDQL ENVGHGEKAL AGGKEAGK

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	AL939111 Genomic DNA. Translation: CAB39882.1.
PIR	T35537.
RefSeq	NP_626411.1.
3D structure databases
HSSP	HSSP built from PDB template 1FFT based on UniProtKB P18401.
ModBase	Search...
Genome annotation databases
GeneID	1097589.
GenomeReviews	Gene locus SCO2155 in contig AL645882_GR.
KEGG	sco:SCO2155.
NMPDR	fig|100226.1.peg.2121.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9X813.
OMA	MTFLPMH.
Enzyme and pathway databases
BioCyc	SCOE100226:SCO2155-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

COX1A_STRCO

Accession

Primary (citable) accession number: Q9X813

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	November 1, 1999
Last modified:	November 3, 2009
This is version 58 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)