ID C0QJE8_DESAH Unreviewed; 635 AA.
AC C0QJE8;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=AcsA2 {ECO:0000313|EMBL:ACN15961.1};
DE EC=6.2.1.1 {ECO:0000313|EMBL:ACN15961.1};
GN Name=acsA2 {ECO:0000313|EMBL:ACN15961.1};
GN OrderedLocusNames=HRM2_28730 {ECO:0000313|EMBL:ACN15961.1};
OS Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS HRM2) (Desulfobacterium autotrophicum).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulforapulum.
OX NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN15961.1, ECO:0000313|Proteomes:UP000000442};
RN [1] {ECO:0000313|EMBL:ACN15961.1, ECO:0000313|Proteomes:UP000000442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC {ECO:0000313|Proteomes:UP000000442};
RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA Meyerdierks A., Gottschalk G., Amann R.;
RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT reducer oxidizing organic carbon completely to carbon dioxide.";
RL Environ. Microbiol. 11:1038-1055(2009).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; CP001087; ACN15961.1; -; Genomic_DNA.
DR RefSeq; WP_015904723.1; NC_012108.1.
DR AlphaFoldDB; C0QJE8; -.
DR STRING; 177437.HRM2_28730; -.
DR KEGG; dat:HRM2_28730; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_3_5_7; -.
DR OrthoDB; 9801302at2; -.
DR Proteomes; UP000000442; Chromosome.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
DR CDD; cd05967; PrpE; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR43347; ACYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR43347:SF3; ACYL-COA SYNTHETASE SHORT-CHAIN FAMILY MEMBER 3, MITOCHONDRIAL; 1.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:ACN15961.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000442}.
FT DOMAIN 5..59
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 73..446
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 512..590
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 635 AA; 70336 MW; B2C43B9D843DA036 CRC64;
MSNLYEEAYN QSINDPEAFW GPIAEECHWY KKWDKVLDDS NKPFYRWFVG GEMNTCYNAL
DLHIDNGIGE NKALIYDSPV TNTKRVYTFN ELRDEVARFA GVLAAKNVQK GDRVIIYMPM
IPEAAIAMLA CARLGAVHSV VFGGFAANEL ATRINDAKPK VMVTASCGIE VKKVIPYKPL
LDESINLAGF KPDSCIVFQR PMVQAELKAG RDYDWDELMN AAKPHDCVPV LATDPLYILY
TSGTTGQPKG VVRDNGGHLV ALKWTMKAIY DIDEGDVYWA ASDIGWVVGH SYIVYAPLFK
GATTIMFEGK PVGTPDAGTF WRVIQDHGVK SLFTAPTAFR AIKRDDPEAK LMKDYDLSSF
KILFLAGERT DSDTLKWAET NLKVPVIDHW WQTETGWAIA ANCMGLHHFP VKPGSPTKAV
PGWDVQVVDP NNKPVASGEI GAIVVKLPLP PGTLPTLWQN DKRYIEAYLE EFPGYYKTAD
AGYIDEEGYI YVMTRTDDII NVAGHRLSTG AMEEVLSCHP MVAECAVMGV EDRLKGQVPL
GFLVLKAGVT VDHDQIIREA IQMVRDQIGP VAAFKTATIV KRLPKTRSGK ILRGTMRSIA
DQKEYKVPAT IDDPAILDEI EVSLGAIGYG KKASK
//
