Reviewed, UniProtKB/Swiss-Prot Q9F8A8 (COOS2_CARHZ)

Names and origin

Protein names

Recommended name:
    Carbon monoxide dehydrogenase 2
      Short name=CODH 2
    EC=1.2.99.2

Gene names

Name:	cooS2
Synonyms:	cooSII
Ordered Locus Names:	CHY_0085

Organism

Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008) [Complete proteome] [HAMAP]

Taxonomic identifier

246194 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteriaceae › Carboxydothermus

Protein attributes

Sequence length	636 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	CODH oxidizes carbon monoxide coupled, via cooF, to the reduction of a hydrogen cation by a hydrogenase (possibly cooH) By similarity.
Catalytic activity	CO + H2O + A = CO2 + AH2.
Cofactor	Binds 3 4Fe-4S clusters per homodimer. Binds 2 nickel-iron-sulfur clusters per homodimer.
Enzyme regulation	Inactivated by O2.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Note: Loosely attached to the inner membrane, probably via cooF. Ref.3
Domain	Cluster B is an all-cysteinyl-liganded 4Fe4S cluster; cluster C is a mixed Ni-Fe-S cluster which appears to be the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe4S cluster that bridges the two subunits of the CODH dimer.
Sequence similarities	Belongs to the Ni-containing carbon monoxide dehydrogenase family.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Cytoplasm Membrane
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding Nickel
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	generation of precursor metabolites and energy Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW carbon-monoxide dehydrogenase (acceptor) activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW nickel ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.3

Chain

2 – 636

635

Carbon monoxide dehydrogenase 2

PRO_0000157138

Sites

Metal binding

39

1

Iron-sulfur 1 (4Fe-4S); shared with dimeric partner

Metal binding

47

1

Iron-sulfur 1 (4Fe-4S); shared with dimeric partner

Metal binding

48

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

51

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

56

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

70

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

261

1

Nickel-iron-sulfur (Ni-4Fe-5S); via tele nitrogen

Metal binding

295

1

Nickel-iron-sulfur (Ni-4Fe-5S)

Metal binding

333

1

Nickel-iron-sulfur (Ni-4Fe-5S)

Metal binding

446

1

Nickel-iron-sulfur (Ni-4Fe-5S)

Metal binding

476

1

Nickel-iron-sulfur (Ni-4Fe-5S)

Metal binding

526

1

Nickel-iron-sulfur (Ni-4Fe-5S)

Experimental info

Sequence conflict

528

1

D → H in AAG29809. Ref.1

Sequence conflict

532

1

A → S in AAG29809. Ref.1

Sequence conflict

544

1

G → W in AAG29809. Ref.1

Sequence conflict

547

1

L → M in AAG29809. Ref.1

Sequence conflict

558

1

E → Q in AAG29809. Ref.1

Sequence conflict

583

1

L → F in AAG29809. Ref.1

Sequence conflict

615 – 617

3

ETA → VQQR in AAG29809. Ref.1

Sequence conflict

636

1

W → R in AAG29809. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

636

Helix Strand Turn

Details...

Turn

5 – 7

3

Helix

11 – 23

13

Helix

28 – 35

8

Helix

40 – 44

5

Beta strand

60 – 64

5

Helix

74 – 108

35

Helix

120 – 130

11

Helix

139 – 152

14

Helix

162 – 165

4

Helix

170 – 178

9

Helix

186 – 196

11

Helix

205 – 234

30

Beta strand

240 – 245

6

Helix

246 – 248

3

Beta strand

253 – 261

9

Helix

263 – 275

13

Helix

277 – 282

6

Beta strand

288 – 293

6

Helix

294 – 304

11

Beta strand

308 – 310

3

Helix

312 – 314

3

Helix

315 – 320

6

Beta strand

324 – 329

6

Beta strand

331 – 333

3

Helix

337 – 345

9

Beta strand

348 – 351

4

Beta strand

361 – 363

3

Helix

368 – 370

3

Helix

371 – 388

18

Turn

389 – 391

3

Beta strand

401 – 405

5

Helix

409 – 417

9

Helix

425 – 434

10

Beta strand

435 – 437

3

Beta strand

440 – 443

4

Helix

455 – 466

12

Beta strand

470 – 474

5

Helix

475 – 483

9

Turn

484 – 487

4

Helix

489 – 491

3

Helix

492 – 495

4

Helix

498 – 510

13

Beta strand

519 – 526

8

Helix

529 – 543

15

Helix

547 – 549

3

Beta strand

550 – 556

7

Helix

562 – 574

13

Beta strand

577 – 580

4

Turn

585 – 588

4

Helix

590 – 597

8

Turn

598 – 600

3

Helix

601 – 604

4

Beta strand

607 – 610

4

Helix

614 – 631

18

Sequences

	Sequence		Length	Mass (Da)
	Q9F8A8-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 61C1011E86022A63	FASTA	636	66,914
	10 20 30 40 50 60 MAKQNLKSTD RAVQQMLDKA KREGIQTVWD RYEAMKPQCG FGETGLCCRH CLQGPCRINP 70 80 90 100 110 120 FGDEPKVGIC GATAEVIVAR GLDRSIAAGA AGHSGHAKHL AHTLKKAVQG KAASYMIKDR 130 140 150 160 170 180 TKLHSIAKRL GIPTEGQKDE DIALEVAKAA LADFHEKDTP VLWVTTVLPP SRVKVLSAHG 190 200 210 220 230 240 LIPAGIDHEI AEIMHRTSMG CDADAQNLLL GGLRCSLADL AGCYMGTDLA DILFGTPAPV 250 260 270 280 290 300 VTESNLGVLK ADAVNVAVHG HNPVLSDIIV SVSKEMENEA RAAGATGINV VGICCTGNEV 310 320 330 340 350 360 LMRHGIPACT HSVSQEMAMI TGALDAMILD YQCIQPSVAT IAECTGTTVI TTMEMSKITG 370 380 390 400 410 420 ATHVNFAEEA AVENAKQILR LAIDTFKRRK GKPVEIPNIK TKVVAGFSTE AIINALSKLN 430 440 450 460 470 480 ANDPLKPLID NVVNGNIRGV CLFAGCNNVK VPQDQNFTTI ARKLLKQNVL VVATGCGAGA 490 500 510 520 530 540 LMRHGFMDPA NVDELCGDGL KAVLTAIGEA NGLGGPLPPV LHMGSCVDNS RAVALVAALA 550 560 570 580 590 600 NRLGVDLDRL PVVASAAEAM HEKAVAIGTW AVTIGLPTHI GVLPPITGSL PVTQILTSSV 610 620 630 KDITGGYFIV ELDPETAADK LLAAINERRA GLGLPW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genetic analysis of Carboxydothermus hydrogenoformans carbon monoxide dehydrogenase genes cooF and cooS." Gonzalez J.M., Robb F.T. FEMS Microbiol. Lett. 191:243-247(2000) [PubMed: 11024270] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Life in hot carbon monoxide: the complete genome sequence of Carboxydothermus hydrogenoformans Z-2901." Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J., Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A. PLoS Genet. 1:563-574(2005) [PubMed: 16311624] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Two membrane-associated NiFeS-carbon monoxide dehydrogenases from the anaerobic carbon-monoxide-utilizing eubacterium Carboxydothermus hydrogenoformans." Svetlitchnyi V., Peschel C., Acker G., Meyer O. J. Bacteriol. 183:5134-5144(2001) [PubMed: 11489867] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21, SUBCELLULAR LOCATION.
[4]	"A genomic survey of the extreme thermophilic, CO-utilizing bacterium Carboxydothermus hydrogenoformans." Gonzalez J.M., Robb F.T. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 217-429.
[5]	"Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster." Dobbek H., Svetlitchnyi V., Gremer L., Huber R., Meyer O. Science 293:1281-1285(2001) [PubMed: 11509720] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF249899 Genomic DNA. Translation: AAG29809.1.
CP000141 Genomic DNA. Translation: ABB15588.1.
AF244619 Genomic DNA. Translation: AAG23568.1.

RefSeq

YP_358957.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SU6	X-ray	1.64	A	2-635	[»]
1SU7	X-ray	1.12	A	2-635	[»]
1SU8	X-ray	1.10	A	2-635	[»]
1SUF	X-ray	1.15	A	2-635	[»]
3B51	X-ray	1.40	X	1-636	[»]
3B52	X-ray	1.50	X	1-636	[»]
3B53	X-ray	1.50	X	1-636	[»]
3I39	X-ray	1.36	X	1-636	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q9F8A8.

Genome annotation databases

GeneID

3727694.

GenomeReviews

Gene locus CHY_0085 in contig CP000141_GR.

KEGG

chy:CHY_0085.

NMPDR

fig|246194.3.peg.655.

TIGR

CHY_0085.

Phylogenomic databases

eggNOG

COG1151.

HOGENOM

HBG393174.

OMA

AIGEANG.

Enzyme and pathway databases

BioCyc

CHYD246194:CHY_0085-MONOMER.

Family and domain databases

InterPro

IPR016101. CO_DH_a-bundle.
IPR010047. CO_DH_cat.
IPR004137. Prismane.
IPR011254. Prismane-like.
IPR016099. Prismane-like_a/b-sand.
[Graphical view]

Gene3D

G3DSA:1.20.1270.30. CO_DH_a-bundle. 1 hit.
G3DSA:3.40.50.2030. Prismane-like_a/b-sand. 1 hit.

Pfam

PF03063. Prismane. 1 hit.
[Graphical view]

PIRSF

PIRSF005023. CODH. 1 hit.

TIGRFAMs

TIGR01702. CO_DH_cata. 1 hit.

ProtoNet

Search...

Entry information

Entry name

COOS2_CARHZ

Accession

Primary (citable) accession number: Q9F8A8
Secondary accession number(s): Q3AFX7, Q9F8L4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2003
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 67 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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