ACSC_MOOTH
ID ACSC_MOOTH Reviewed; 446 AA.
AC Q07340;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Corrinoid/iron-sulfur protein large subunit;
DE Short=C/Fe-SP large subunit;
DE Short=CFeSP large subunit;
GN Name=acsC;
OS Moorella thermoacetica (Clostridium thermoaceticum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=1525;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RX PubMed=8449924; DOI=10.1016/s0021-9258(18)53364-0;
RA Lu W.-P., Schiau I., Cunningham J.R., Ragsdale S.W.;
RT "Sequence and expression of the gene encoding the corrinoid/iron-sulfur
RT protein from Clostridium thermoaceticum and reconstitution of the
RT recombinant protein to full activity.";
RL J. Biol. Chem. 268:5605-5614(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8, PROTEIN SEQUENCE OF 2-19, AND
RP FUNCTION.
RC STRAIN=ATCC 35608 / DSM 521 / JCM 9319;
RX PubMed=2911576; DOI=10.1073/pnas.86.1.32;
RA Roberts D.L., James-Hagstrom J.E., Garvin D.K., Gorst C.M., Runquist J.A.,
RA Baur J.R., Haase F.C., Ragsdale S.W.;
RT "Cloning and expression of the gene cluster encoding key proteins involved
RT in acetyl-CoA synthesis in Clostridium thermoaceticum: CO dehydrogenase,
RT the corrinoid/Fe-S protein, and methyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:32-36(1989).
RN [3]
RP FUNCTION, COFACTOR, AND 5-METHOXYBENZIMIDAZOLYLCOBAMIDE-BINDING.
RX PubMed=2821001; DOI=10.1016/s0021-9258(18)47936-7;
RA Ragsdale S.W., Lindahl P.A., Muenck E.;
RT "Moessbauer, EPR, and optical studies of the corrinoid/iron-sulfur protein
RT involved in the synthesis of acetyl coenzyme A by Clostridium
RT thermoaceticum.";
RL J. Biol. Chem. 262:14289-14297(1987).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) IN COMPLEX WITH ACSC; ACSE;
RP COBALAMIN AND IRON-SULFUR, COFACTOR, FUNCTION, AND SUBUNIT.
RX PubMed=22419154; DOI=10.1038/nature10916;
RA Kung Y., Ando N., Doukov T.I., Blasiak L.C., Bender G., Seravalli J.,
RA Ragsdale S.W., Drennan C.L.;
RT "Visualizing molecular juggling within a B12-dependent methyltransferase
RT complex.";
RL Nature 484:265-269(2012).
CC -!- FUNCTION: Acts as a methyl group carrier in the anaerobic acetyl-CoA
CC pathway (Wood-Ljungdahl pathway) of carbon monoxide and carbon dioxide
CC fixation. Binds the corrinoid 5-methoxybenzimidazolylcobamide which is
CC then methylated by the AcsE subunit (PubMed:2821001).
CC {ECO:0000269|PubMed:22419154, ECO:0000269|PubMed:2821001,
CC ECO:0000269|PubMed:2911576, ECO:0000269|PubMed:8449924}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:22419154, ECO:0000269|PubMed:2821001};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:22419154,
CC ECO:0000269|PubMed:2821001};
CC -!- SUBUNIT: Heterohexamer composed of 2 subunits of AcsC, 2 subunits of
CC AcsD and 2 subunits of AcsE. {ECO:0000269|PubMed:22419154}.
CC -!- INTERACTION:
CC Q07340; Q07341: acsD; NbExp=2; IntAct=EBI-15974900, EBI-15974920;
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DR EMBL; L07099; AAA23254.1; -; Genomic_DNA.
DR PIR; A46621; A46621.
DR RefSeq; WP_011392715.1; NZ_VCDY01000001.1.
DR PDB; 4DJD; X-ray; 2.38 A; C/E=1-446.
DR PDB; 4DJE; X-ray; 3.50 A; C/E=1-446.
DR PDB; 4DJF; X-ray; 3.03 A; C/E=1-446.
DR PDBsum; 4DJD; -.
DR PDBsum; 4DJE; -.
DR PDBsum; 4DJF; -.
DR AlphaFoldDB; Q07340; -.
DR SMR; Q07340; -.
DR DIP; DIP-59669N; -.
DR IntAct; Q07340; 2.
DR OMA; SCMAFAT; -.
DR OrthoDB; 875842at2; -.
DR BioCyc; MetaCyc:COEBETACLTH-MON; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0031419; F:cobalamin binding; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR GO; GO:0046356; P:acetyl-CoA catabolic process; IEA:InterPro.
DR GO; GO:0015977; P:carbon fixation; IDA:UniProtKB.
DR Gene3D; 3.20.20.20; -; 1.
DR InterPro; IPR007202; 4Fe-4S_dom.
DR InterPro; IPR016041; Ac-CoA_synth_d_su_TIM-brl.
DR InterPro; IPR016218; AcylCoA_decarb/synth_gsu.
DR InterPro; IPR011005; Dihydropteroate_synth-like.
DR Pfam; PF03599; CdhD; 1.
DR Pfam; PF04060; FeS; 1.
DR PIRSF; PIRSF000376; AcCoA_decarb_gamma; 1.
DR SUPFAM; SSF51717; SSF51717; 1.
DR PROSITE; PS51656; 4FE4S; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Carbon dioxide fixation; Cobalt;
KW Direct protein sequencing; Iron; Iron-sulfur; Metal-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..446
FT /note="Corrinoid/iron-sulfur protein large subunit"
FT /id="PRO_0000064441"
FT DOMAIN 2..59
FT /note="4Fe-4S"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00989"
FT BINDING 17
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:22419154,
FT ECO:0007744|PDB:4DJD"
FT BINDING 20
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:22419154,
FT ECO:0007744|PDB:4DJD"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:22419154,
FT ECO:0007744|PDB:4DJD"
FT BINDING 42
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:22419154,
FT ECO:0007744|PDB:4DJD"
FT BINDING 340
FT /ligand="5-methoxybenzimidazolylcob(I)amide"
FT /ligand_id="ChEBI:CHEBI:157765"
FT /evidence="ECO:0000305|PubMed:22419154,
FT ECO:0007744|PDB:4DJD"
FT BINDING 346
FT /ligand="5-methoxybenzimidazolylcob(I)amide"
FT /ligand_id="ChEBI:CHEBI:157765"
FT /evidence="ECO:0000305|PubMed:22419154,
FT ECO:0007744|PDB:4DJD"
FT BINDING 370..373
FT /ligand="5-methoxybenzimidazolylcob(I)amide"
FT /ligand_id="ChEBI:CHEBI:157765"
FT /evidence="ECO:0000305|PubMed:22419154,
FT ECO:0007744|PDB:4DJD"
FT BINDING 433
FT /ligand="5-methoxybenzimidazolylcob(I)amide"
FT /ligand_id="ChEBI:CHEBI:157765"
FT /evidence="ECO:0000305|PubMed:22419154,
FT ECO:0007744|PDB:4DJD"
FT HELIX 5..9
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 141..151
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 165..172
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:4DJD"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 211..223
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 238..254
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 273..285
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 298..311
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:4DJF"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 344..351
FT /evidence="ECO:0007829|PDB:4DJD"
FT TURN 352..358
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:4DJF"
FT HELIX 373..378
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 384..393
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:4DJF"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 414..422
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 436..441
FT /evidence="ECO:0007829|PDB:4DJD"
SQ SEQUENCE 446 AA; 48153 MW; FF9FE2C8B723C550 CRC64;
MPLTGLEIYK QLPKKNCGEC GTPTCLAFAM NLASGKASLD SCPYVSDAAR EALDAAAAPP
IAKVVLGAGP TAVEMGDETE LFRHDKRFYH ETAIAIQVSD NLSSEELKAK VEAINGLNFD
RVGQHYTIQA IAIRHDADDP AAFKAAVASV AAATQLNLVL MADDPDVLKE ALAGVADRKP
LLYAATGANY EAMTALAKEN NCPLAVYGNG LEELAELVDK IVALGHKQLV LDPGARETSR
AIADFTQIRR LAIKKRFRSF GYPIIALTTA ANPLDEVLQA VNYVTKYASL VVLRTDAKEH
LLPLLSWRQN LYTDPQVPIR VEEKLNEIGA VNENSPVYVT TNFSLTYYSV EGEIESTKIP
SYLLSVDTDG LSVLTAYADG KFEAEKIAAV MKKVDLDNKV KRHRIIIPGA VAVLKGKLED
LTGWEVIVGP REASGIVAFA RANLAS
