ID I9L7X6_9FIRM Unreviewed; 1458 AA.
AC I9L7X6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Amino acid adenylation domain protein {ECO:0000313|EMBL:EIW16351.1};
GN ORFNames=FB4_0862 {ECO:0000313|EMBL:EIW16351.1};
OS Pelosinus fermentans B4.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Pelosinus.
OX NCBI_TaxID=1149862 {ECO:0000313|EMBL:EIW16351.1, ECO:0000313|Proteomes:UP000004324};
RN [1] {ECO:0000313|EMBL:EIW16351.1, ECO:0000313|Proteomes:UP000004324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:EIW16351.1,
RC ECO:0000313|Proteomes:UP000004324};
RX PubMed=22933770; DOI=10.1128/JB.01174-12;
RA Brown S.D., Podar M., Klingeman D.M., Johnson C.M., Yang Z.K.,
RA Utturkar S.M., Land M.L., Mosher J.J., Hurt R.A.Jr., Phelps T.J.,
RA Palumbo A.V., Arkin A.P., Hazen T.C., Elias D.A.;
RT "Draft Genome Sequences for Two Metal-Reducing Pelosinus fermentans Strains
RT Isolated from a Cr(VI)-Contaminated Site and for Type Strain R7.";
RL J. Bacteriol. 194:5147-5148(2012).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIW16351.1}.
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DR EMBL; AKVJ01000066; EIW16351.1; -; Genomic_DNA.
DR RefSeq; WP_007937343.1; NZ_AKVJ01000066.1.
DR PATRIC; fig|1149862.3.peg.3865; -.
DR OrthoDB; 9765680at2; -.
DR Proteomes; UP000004324; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd12114; A_NRPS_TlmIV_like; 1.
DR CDD; cd19535; Cyc_NRPS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 1.10.10.1830; Non-ribosomal peptide synthase, adenylation domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR036736; ACP-like_sf.
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 InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR041464; TubC_N.
DR InterPro; IPR044894; TubC_N_sf.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR PANTHER; PTHR45527:SF15; PYOCHELIN SYNTHASE PCHF; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR Pfam; PF18563; TubC_N; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 1044..1128
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1458 AA; 162187 MW; 637578435017718C CRC64;
MIPNCKININ SLVARLRGEG VSLWAENGKL RYRAPQGMLA GSDLQSLKDY KTNILSLLQS
EAKPVTVEYH PESRYEPFPL TDVQFAYLLG RSEVFGYGGV ACHIYLELNY PELERRRVEA
AWNKLVLRHD MLRAVINKNG YQQVMEKVPR LDVAYTDAGA WETDKVSAQL DDIREEMGHR
IYNTDCWPLF GVAVTKTPDR AVLHFSIEFL IADWASIWLL LSEFEALYYE PERMLPDFKL
SFRDYLIAER SLRESIVYAK DKDYWFRRID DLPLAPDLPM ARFQTNFGQA RFSRRFLKLD
AQSWNGLKQK AQQRGLTPTA AVMTAYAAVL ERWSRNKKFC LNLTVLNRLP LHSQVNDIVG
DFTSVSLLAV DWYTGNSFTE RAKTMNKQLF EDLDHRLFSG VEVLREISRR RGREAALMPI
VFTSAIGLVE PTEGNCLQGK VEGQGISQTP QVFIDCQAMD SSSGLQVNWD IREGVFPEGM
TDDMFDAFES LLRLLGGMQQ VWDAGETAAL PAWQLSERQR VNDTKMTLPD GLLHSGILAQ
AAATPDRPAV LDSKGQVTYG ELMLIASAVA GKLQETGCKQ QDRVAIIMDK SVHQVAAVLG
ALSAGAVYVP VDTTQPELRR SAMLKKTNVL HVLTCSTSGI KWPENITVIE VDKLTPHREN
ALVADYDPDM PAYIIHTSGS TGQPKGVVIT HRAAANTITD INSRFKVGRD DKVLGLAQLS
FDLSVYDIFG ILSAGGTLIY PSADRQTDPS HWVELMAEHE ITVWNSVPAL VQMLVAYLNS
ESKIDLAKFR LAMLSGDWIP LTLPDTLIKR VPSVQVISLG GATEASIWSN YHVYQGLQPD
WSSIPYGRPL ANQGFRILDE RLRDCPVWVM GGLYITGDGL AKGYFGDKET TEARFFPHHV
DGQRLYHTGD MGRYMPGGEI EFLGREDNQV KIKGHRIELG EIEAALQKHP AVAAAAVVVD
SSGDNKALIG IVETVCFKQN SIPVNAATLA DFLSQRLPAY MIPAAIQIVD ALPLTGNGKI
DRRELAKWKI QSITDDSVME SIAGISDPLE EQLLRIWAEA LGMPVIGRLQ NFYDHGADSL
IMAQVAGKLR EIFAGESLML DIPFDALLRQ MLNYPTVAAL AEFVRLQSNK TGHASVDDSI
RQQKNNSSNA VLTSYGGGTG ALRVVFHAGL GTMNCFRQLL THLDEQNSGP VIGITVADTD
LYCSLDHSGL IEHLADDYAE RLIETGHKEM QLIGYSLGGL IAVEVARRLL EKGIHLLDLV
LIDSPPVLYD IDDNLVIESL FIQNLHIPLE KAGFSSVNQD EFVRGLRHMF EVNNHSIPAG
ASLAIGGDEG LDKVGDLFRR LSVLSTRDRF TVYVEAVAKV TGDKMPVEMA EGMFKVFRQS
LKSAHFTPQP YMGDIRFLLA REPFALMPWT NETTLGFWKE ICLGKFSVQK IAGNHFTCIV
AEPNASDLAR VIGDLQCR
//
