P27988 (DCMA_MOOTH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit alpha Short name=ACS subunit Short name=Acetyl-CoA synthase subunit Short name=CODH/ACS EC=2.3.1.169
Organism	Moorella thermoacetica (Clostridium thermoaceticum)
Taxonomic identifier	1525 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteriaceae › Moorella group › Moorella

Protein attributes

Sequence length	729 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The beta subunit generates CO from CO2, while the alpha subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the alpha subunit by a corrinoid iron-sulfur protein.
Catalytic activity	Acetyl-CoA + corrinoid protein = CO + methylcorrinoid protein + CoA.
Cofactor	Binds 2 nickel ions per subunit. Binds 1 4Fe-4S cluster per subunit.
Subunit structure	Tetramer of two alpha and two beta chains.

Ontologies

Keywords
Biological process	Carbon dioxide fixation
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding Nickel
Molecular function	Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	acetyl-CoA metabolic process Inferred from electronic annotation. Source: InterPro carbon fixation Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW CO-methylating acetyl-CoA synthase activity Inferred from electronic annotation. Source: EC carbon-monoxide dehydrogenase (acceptor) activity Inferred from electronic annotation. Source: InterPro metal 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

Chain

1 – 729

729

Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit alpha

PRO_0000079807

Sites

Metal binding

506

1

Iron-sulfur (4Fe-4S)

Metal binding

509

1

Iron-sulfur (4Fe-4S)

Metal binding

509

1

Nickel 1

Metal binding

518

1

Iron-sulfur (4Fe-4S)

Metal binding

528

1

Iron-sulfur (4Fe-4S)

Metal binding

595

1

Nickel 1

Metal binding

595

1

Nickel 2

Metal binding

596

1

Nickel 1; via amide nitrogen

Metal binding

596

1

Nickel 2; via amide nitrogen

Metal binding

597

1

Nickel 1

Metal binding

597

1

Nickel 2

Secondary structure

1

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729

Helix Strand Turn

Details...

Helix

4 – 8

5

Helix

19 – 47

29

Beta strand

59 – 62

4

Helix

63 – 68

6

Helix

76 – 78

3

Helix

79 – 88

10

Helix

96 – 117

22

Helix

118 – 120

3

Helix

138 – 143

6

Helix

145 – 148

4

Turn

149 – 151

3

Beta strand

156 – 161

6

Helix

166 – 178

13

Beta strand

182 – 186

5

Helix

189 – 195

7

Helix

202 – 204

3

Beta strand

206 – 211

6

Helix

212 – 215

4

Helix

216 – 228

13

Helix

237 – 247

11

Beta strand

250 – 257

8

Helix

260 – 271

12

Beta strand

276 – 280

5

Helix

284 – 286

3

Turn

289 – 291

3

Beta strand

292 – 294

3

Turn

298 – 300

3

Helix

301 – 309

9

Helix

326 – 328

3

Helix

335 – 337

3

Beta strand

338 – 343

6

Beta strand

349 – 355

7

Helix

358 – 360

3

Beta strand

366 – 370

5

Helix

373 – 375

3

Beta strand

384 – 391

8

Helix

397 – 412

16

Beta strand

417 – 419

3

Beta strand

427 – 431

5

Helix

432 – 437

6

Helix

442 – 455

14

Beta strand

460 – 468

9

Helix

471 – 493

23

Turn

497 – 499

3

Beta strand

501 – 506

6

Helix

508 – 511

4

Beta strand

518 – 521

4

Helix

533 – 542

10

Beta strand

550 – 552

3

Beta strand

555 – 558

4

Turn

559 – 562

4

Helix

565 – 574

10

Beta strand

587 – 590

4

Beta strand

599 – 605

7

Helix

606 – 608

3

Beta strand

610 – 615

6

Helix

628 – 635

8

Beta strand

644 – 647

4

Helix

649 – 653

5

Turn

655 – 658

4

Helix

659 – 661

3

Helix

663 – 666

4

Beta strand

667 – 669

3

Helix

672 – 688

17

Helix

695 – 698

4

Turn

702 – 704

3

Helix

708 – 717

10

Helix

721 – 724

4

Sequences

	Sequence		Length	Mass (Da)
	P27988 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 619BB19D959F5A72	FASTA	729	81,725
	10 20 30 40 50 60 MTDFDKIFEG AIPEGKEPVA LFREVYHGAI TATSYAEILL NQAIRTYGPD HPVGYPDTAY 70 80 90 100 110 120 YLPVIRCFSG EEVKKLGDLP PILNRKRAQV SPVLNFENAR LAGEATWYAA EIIEALRYLK 130 140 150 160 170 180 YKPDEPLLPP PWTGFIGDPV VRRFGIKMVD WTIPGEAIIL GRAKDSKALA KIVKELMGMG 190 200 210 220 230 240 FMLFICDEAV EQLLEENVKL GIDYIAYPLG NFTQIVHAAN YALRAGMMFG GVTPGAREEQ 250 260 270 280 290 300 RDYQRRRIRA FVLYLGEHDM VKTAAAFGAI FTGFPVITDQ PLPEDKQIPD WFFSVEDYDK 310 320 330 340 350 360 IVQIAMETRG IKLTKIKLDL PINFGPAFEG ESIRKGDMYV EMGGNRTPAF ELVRTVSESE 370 380 390 400 410 420 ITDGKIEVIG PDIDQIPEGS KLPLGILVDI YGRKMQADFE GVLERRIHDF INYGEGLWHT 430 440 450 460 470 480 GQRNINWLRV SKDAVAKGFR FKNYGEILVA KMKEEFPAIV DRVQVTIFTD EAKVKEYMEV 490 500 510 520 530 540 AREKYKERDD RMRGLTDETV DTFYSCVLCQ SFAPNHVCIV TPERVGLCGA VSWLDAKASY 550 560 570 580 590 600 EINHAGPNQP IPKEGEIDPI KGIWKSVNDY LYTASNRNLE QVCLYTLMEN PMTSCGCFEA 610 620 630 640 650 660 IMAILPECNG IMITTRDHAG MTPSGMTFST LAGMIGGGTQ TPGFMGIGRT YIVSKKFISA 670 680 690 700 710 720 DGGIARIVWM PKSLKDFLHD EFVRRSVEEG LGEDFIDKIA DETIGTTVDE ILPYLEEKGH PALTMDPIM

References

[1]	"The primary structure of the subunits of carbon monoxide dehydrogenase/acetyl-CoA synthase from Clostridium thermoaceticum." Morton T.A., Runquist J.A., Ragsdale S.W., Shanmugasundaram T., Wood H.G., Ljungdahl L.G. J. Biol. Chem. 266:23824-23828(1991) [PubMed: 1748656] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Identification of a cysteine involved in the interaction between carbon monoxide dehydrogenase and corrinoid/Fe-S protein from Clostridium thermoaceticum." Shanmugasundaram T., Sundaresh C.S., Kumar G.K. FEBS Lett. 326:281-284(1993) [PubMed: 8325380] [Abstract] Cited for: PROTEIN SEQUENCE OF 494-508.
[3]	"A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase." Doukov T.I., Iverson T.M., Seravalli J., Ragsdale S.W., Drennan C.L. Science 298:567-572(2002) [PubMed: 12386327] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[4]	"Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase." Darnault C., Volbeda A., Kim E.J., Legrand P., Vernede X., Lindahl P.A., Fontecilla-Camps J.-C. Nat. Struct. Biol. 10:271-279(2003) [PubMed: 12627225] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M62727 Genomic DNA. Translation: AAA23229.1.

PIR

B41670.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MJG	X-ray	2.20	M/N/O/P	1-729	[»]
1OAO	X-ray	1.90	C/D	1-729	[»]
2Z8Y	X-ray	2.51	M/N/O/P	1-729	[»]
3GIT	X-ray	3.00	A/B/C/D/E/F	311-729	[»]
3I01	X-ray	2.15	M/N/O/P	1-729	[»]
3I04	X-ray	2.15	M/N/O/P	2-729	[»]
3S2X	X-ray	2.35	A/B	594-729	[»]

ProteinModelPortal

P27988.

SMR

P27988. Positions 1-729.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:CODHALPHACLTH-MONOMER.

Family and domain databases

InterPro

IPR004461. CO_DH/Ac-CoA_synth_bsu.
IPR011254. Prismane-like.
IPR016099. Prismane-like_a/b-sand.
[Graphical view]

Gene3D

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

Pfam

PF03598. CdhC. 1 hit.
[Graphical view]

SUPFAM

SSF56821. Prismane_like. 1 hit.

TIGRFAMs

TIGR00316. CdhC. 1 hit.

ProtoNet

Search...

Entry information

Entry name

DCMA_MOOTH

Accession

Primary (citable) accession number: P27988

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	October 19, 2011
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program