ACSD_MOOTH
ID ACSD_MOOTH Reviewed; 323 AA.
AC Q07341;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Corrinoid/iron-sulfur protein small subunit;
DE Short=C/Fe-SP small subunit;
DE Short=CFeSP small subunit;
GN Name=acsD;
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 29-53, PROTEIN SEQUENCE OF 30-63, 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 X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) IN COMPLEX WITH ACSC; ACSE AND
RP COBALAMIN, 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. {ECO:0000269|PubMed:22419154, ECO:0000269|PubMed:2911576,
CC ECO:0000269|PubMed:8449924}.
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 Q07341; Q07340: acsC; NbExp=2; IntAct=EBI-15974920, EBI-15974900;
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DR EMBL; L07100; AAA23255.1; -; Genomic_DNA.
DR PIR; B46621; B46621.
DR RefSeq; WP_011392712.1; NZ_VCDY01000001.1.
DR PDB; 4DJD; X-ray; 2.38 A; D/F=1-323.
DR PDB; 4DJE; X-ray; 3.50 A; D/F=1-323.
DR PDB; 4DJF; X-ray; 3.03 A; D/F=1-323.
DR PDBsum; 4DJD; -.
DR PDBsum; 4DJE; -.
DR PDBsum; 4DJF; -.
DR AlphaFoldDB; Q07341; -.
DR SMR; Q07341; -.
DR DIP; DIP-59670N; -.
DR IntAct; Q07341; 1.
DR GeneID; 61289916; -.
DR OMA; VMDPTTC; -.
DR OrthoDB; 1148398at2; -.
DR BioCyc; MetaCyc:COEALPHACLTH-MON; -.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0015977; P:carbon fixation; IDA:UniProtKB.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.20; -; 1.
DR InterPro; IPR016041; Ac-CoA_synth_d_su_TIM-brl.
DR InterPro; IPR004486; CO_DH/Ac-CoA_synth_dsu.
DR InterPro; IPR011005; Dihydropteroate_synth-like.
DR Pfam; PF03599; CdhD; 1.
DR SUPFAM; SSF51717; SSF51717; 1.
DR TIGRFAMs; TIGR00381; cdhD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbon dioxide fixation; Cobalamin; Cobalt;
KW Direct protein sequencing.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..323
FT /note="Corrinoid/iron-sulfur protein small subunit"
FT /id="PRO_0000064443"
FT BINDING 188
FT /ligand="5-methoxybenzimidazolylcob(I)amide"
FT /ligand_id="ChEBI:CHEBI:157765"
FT /evidence="ECO:0000269|PubMed:22419154,
FT ECO:0007744|PDB:4DJD"
FT CONFLICT 53
FT /note="R -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:4DJD"
FT TURN 76..80
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:4DJD"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 140..153
FT /evidence="ECO:0007829|PDB:4DJD"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:4DJF"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:4DJD"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:4DJD"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 224..240
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 253..258
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:4DJD"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 276..292
FT /evidence="ECO:0007829|PDB:4DJD"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:4DJD"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:4DJD"
FT HELIX 304..317
FT /evidence="ECO:0007829|PDB:4DJD"
SQ SEQUENCE 323 AA; 35070 MW; 51633BDB94036056 CRC64;
MAVQILRDRS RAAVQKVVLG ATKDQGGTRS HTIVVGGDAA LPFHHFEGEI VNRPVIGMEV
QDIVPDWPDV LKDPFTDVIN EPGRWAQKCV AEYGADLIYL KLDGADPEGA NHSVDQCVAT
VKEVLQAVGV PLVVVGCGDV EKDHEVLEAV AEAAAGENLL LGNAEQENYK SLTAACMVHK
HNIIARSPLD INICKQLNIL INEMNLPLDH IVIDPSIGGL GYGIEYSFSI MERIRLGALQ
GDKMLSMPVI CTVGYEAWRA KEASAPVSEY PGWGKETERG ILWEAVTATA LLQAGAHILL
MRHPEAVARV KENIDQLMVS NAY
