Reviewed, UniProtKB/Swiss-Prot Q04440 (COX1_BACPF)

Names and origin

Protein names

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

Gene names

Name:

ctaD

Organism

Bacillus pseudofirmus

Taxonomic identifier

79885 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	625 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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.
Catalytic activity	4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.
Pathway	Energy metabolism; oxidative phosphorylation.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Induction	Elevated expression at high pH.
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	Direct protein sequencing
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
	Initiator methionine	1	1	Removed Ref.1
	Chain	2 – 625	624	Cytochrome c oxidase subunit 1		PRO_0000183434
Regions
	Transmembrane	23 – 43	21	Potential
	Transmembrane	72 – 92	21	Potential
	Transmembrane	99 – 119	21	Potential
	Transmembrane	151 – 171	21	Potential
	Transmembrane	195 – 215	21	Potential
	Transmembrane	240 – 260	21	Potential
	Transmembrane	272 – 292	21	Potential
	Transmembrane	309 – 329	21	Potential
	Transmembrane	343 – 363	21	Potential
	Transmembrane	382 – 402	21	Potential
	Transmembrane	417 – 437	21	Potential
	Transmembrane	460 – 480	21	Potential
	Transmembrane	551 – 571	21	Potential
	Transmembrane	577 – 597	21	Potential
Sites
	Metal binding	69	1	Iron (heme A axial ligand) Probable
	Metal binding	246	1	Copper B Probable
	Metal binding	250	1	Copper B Probable
	Metal binding	295	1	Copper B Probable
	Metal binding	296	1	Copper B Probable
	Metal binding	381	1	Iron (heme A3 axial ligand) Probable
	Metal binding	383	1	Iron (heme A axial ligand) Probable
Amino acid modifications
	Cross-link	246 ↔ 250		1'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q04440-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 6D805E8F9DA1E4A4	FASTA	625	69,885
	10 20 30 40 50 60 MATQKQEKSV IWDWLTTVDH KKIAIMYLIA GTLFFVKAGV MALFMRIQLM YPEMNFLSGQ 70 80 90 100 110 120 TFNEFITMHG TIMLFLAATP LLFAFMNYVI PLQIGARDVA FPFVNALGFW IFFFGGLLLS 130 140 150 160 170 180 LSWFFGGGPD AGWTAYVPLS SRDYGGLGID FYVLGLQVSG IGTLISAINF LVTIVNMRAP 190 200 210 220 230 240 GMTMMRLPLF VWTSFISSTL ILFAFTPLAA GLALLMLDRL FEAQYFIPSM GGNVVLWQHI 250 260 270 280 290 300 FWIFGHPEVY ILVLPAFGII SEVIPAFSRK RLFGYTAMVF ATMIIAFLGF MVWAHHMFTV 310 320 330 340 350 360 GMGPVANSIF AVATMTIAVP TGIKIFNWLF TMWGGKITFN TAMLFASSFV PTFVLGGVTG 370 380 390 400 410 420 VMLAMAPVDY LYHDTYFVVA HFHYIIVGGI VLSLFAGLFY WYPKMFGHML NETLGKLFFW 430 440 450 460 470 480 VFYIGFHLTF FVQHLLGLMG MPRRVYTYLG DQGLDAFNFI STIGTFFMSA GVILLVINVI 490 500 510 520 530 540 YSAFKGERVT VADPWDARTL EWATPTPVPE YNFAQTPQVR SLDPLFYEKI HGDGTMKPAE 550 560 570 580 590 600 PVTDIHMPNG SILPFIMSIG LFFAGFGLIM LNMDKPIINP WIVAIGGLAL TFGCMFVRSI 610 620 KEDHGYHIPA EQVKADLAEL KKGGN

References

[1]

"Cloning of the cta operon from alkaliphilic Bacillus firmus OF4 and characterization of the pH-regulated cytochrome caa3 oxidase it encodes." Quirk P.G., Hicks D.B., Krulwich T.A. J. Biol. Chem. 268:678-685(1993) [PubMed: 7678007] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13. Strain: OF4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M94110 Genomic DNA. Translation: AAA22365.1.
3D structure databases
SMR	Q04440. Positions 18-513.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.9.3.1. 291073.
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

COX1_BACPF

Accession

Primary (citable) accession number: Q04440

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 70 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)