ID K9V2X9_9CYAN Unreviewed; 1803 AA.
AC K9V2X9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Amino acid adenylation domain protein {ECO:0000313|EMBL:AFZ01575.1};
DE EC=5.1.1.13 {ECO:0000313|EMBL:AFZ01575.1};
GN ORFNames=Cal6303_2598 {ECO:0000313|EMBL:AFZ01575.1};
OS Calothrix sp. PCC 6303.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFZ01575.1, ECO:0000313|Proteomes:UP000010477};
RN [1] {ECO:0000313|EMBL:AFZ01575.1, ECO:0000313|Proteomes:UP000010477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6303 {ECO:0000313|EMBL:AFZ01575.1,
RC ECO:0000313|Proteomes:UP000010477};
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003610; AFZ01575.1; -; Genomic_DNA.
DR STRING; 1170562.Cal6303_2598; -.
DR KEGG; calt:Cal6303_2598; -.
DR PATRIC; fig|1170562.3.peg.2848; -.
DR eggNOG; COG0318; Bacteria.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_000022_0_9_3; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000010477; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0047689; F:aspartate racemase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd05931; FAAL; 1.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
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; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR040097; FAAL/FAAC.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:AFZ01575.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010477};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 90..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 623..700
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1701..1776
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1803 AA; 202960 MW; E087EC835D665989 CRC64;
MNQYSHSFKQ ASDAFSVRGY TNNGLDVQDY STVVELLSFR SFTQPNQTAF TYLLDGETEQ
LKLTYQELDR LARRVAAKLQ ELDLTGQRAL LLYPAGLDFL IAFFGCLYAG VVAVTAYPPR
NQRNTPRIQA ISADAQAAIA LTTTEILSTV QSLMTEKTEL QSLQWLTTDN LTEGLEDCWQ
KPNINTNTLA FLQYTSGSTG IPKGVMISHG NLLHNAQTTY QFMEHSPESK FVTWLPMYHD
MGLIGGILQP LYGGFPCLIM PPASFLQRPY RWLQAISRYQ GTTSGGPNFA YDLCVQKITP
EQKATLDLSS WSVAFNGAEP IRHDTLERFA EAFSQCGFRR EAFYPCYGMA ETTLMISGVQ
KATSPQVKSV LRSALESNRV VKSSVTGGNE DPHHFVSCGR IIPGQKVIII NPETLKSCEA
DEIGEIWVSG LSVGQGYWNR QEETADTFDA YVSDTREGPF LRTGDLGFLQ DEELFITGRA
KDLIIIRGRN LYPQDIELTA ERSHSSLRPG ASAAFTVEVS DEEKLVIVQE LEFRARPNIE
EVVNAIRQAV TEEHEVLVYA VVLIKPGSIP KTSSGKIQRC TTCTQFENGE LNIVSSNILK
NKNTTSKSTQ LQGSQLLSLS PKECQALLES YLIEQQGRVL AIASSDIHPE EPLTSLGLDS
LKVFDLKNQI ETDLEVEISV TDLFSGMSTR SLVTKILDQV ATKELPSPPV THHRNNPPTL
TYPLSFTQQG LWFIHQLTPN APTYNIPIII NLKGNLNLPA LQESLNEIIR RHEVLRTSFT
VINQQPVQVI NQPVPLTLNV EKVQTLAQQQ PDSLIQHLTS EFAQQPFDLS VSLPLRTKIC
QINDKNYYLI VTLHHIIADG WSIGVLLKEL ATLYDAFSSG QQPLLPELPN QYRDFVNWQQ
QSLDNECIQP LLSYWREKLQ GDLPVLDLPT DRPRQAVQTF KGAQAKLLLD PNLVKQLNRL
SRQQGVTLFM TLLTAFKILL HKYTDQTDIL VGSPIAGRNR AEVKALIGLF INILVLRTDL
SGDPSFQDLL AQVKSTALEA YVHQDLPLEK LVEDLKPNRD LSYHPLFQVM FVLQSVPKPN
LSLSNRSLSY GEGHNGTSKF DLTLFMEEDS EQGLVATCEY NTDLFNTDTI TRMLGHYQTL
LESIVSQPEQ NISQLQILTQ PEVQQLLIDW NNTKKDYPHA KCIHQLFEEQ VEKTPDAVAV
IFENQKLTYQ ELNTQANQLG NYLQQQGVKP DTVVGIYMER SLSMVVALIA VLKAGGAYLP
LDPSYPHERL AFMLADAQVQ VVLTQSQLGK ELPYQEQLQF VKIEDLVYAN CGIQNLISDV
QPENLAYVIY TSGSTGKPKG VMNTHHGLCN RLLWMQDTYQ LTSADRVLQK TPFSFDVSVW
EFFWTLLTGA VLVVAKPGGH QEPRYLSELI SQQQISVLHF VPSMLQIFLG ETQHQQCKTI
KHVICSGEAL SWDLQQRFFQ SFEAKLHNLY GPTEVSIDVT AWCCKPGNQE SNHENIVPIG
RPIANTQIFI LDRHLKPVPL GVKGELYIGG LGLARGYLNQ PQLTQEKFIP HPFTNLQNLQ
LDGVSTRLYK TGDLARYRPD GNIEFLGRID YQVKIRGNRL ELGEIEALLE QHPQVQETVV
VARQDIANDL RLVAYLVTSG DATLSIDELR GFLKQKLPDY MIPSAFVILE ALPLTLNGKV
DRRSLPTPDN LRPELTAPFQ PPQSVIQQQI AQIWQEVLGV DKVGIHDNFF DLGGHSLLIL
QVNRQLCETF QREISVVTMF QNPTIDSLAE YFSQKQEKKP LFQEIDQRVE KKKQLLKNQR
KKR
//
