ID D3LLK2_MICLU Unreviewed; 747 AA.
AC D3LLK2;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=SAF domain protein {ECO:0000313|EMBL:EFD51666.1};
GN ORFNames=HMPREF0569_0663 {ECO:0000313|EMBL:EFD51666.1};
OS Micrococcus luteus SK58.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Micrococcus.
OX NCBI_TaxID=596312 {ECO:0000313|EMBL:EFD51666.1, ECO:0000313|Proteomes:UP000002933};
RN [1] {ECO:0000313|EMBL:EFD51666.1, ECO:0000313|Proteomes:UP000002933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK58 {ECO:0000313|EMBL:EFD51666.1,
RC ECO:0000313|Proteomes:UP000002933};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
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:EFD51666.1}.
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DR EMBL; ADCD01000021; EFD51666.1; -; Genomic_DNA.
DR RefSeq; WP_002854446.1; NZ_ADCD01000021.1.
DR AlphaFoldDB; D3LLK2; -.
DR Proteomes; UP000002933; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR CDD; cd11615; SAF_NeuB_like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.90.1210.10; Antifreeze-like/N-acetylneuraminic acid synthase C-terminal domain; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1.
DR InterPro; IPR006190; AFP_Neu5c_C.
DR InterPro; IPR036732; AFP_Neu5c_C_sf.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR013132; Neu5Ac_N.
DR InterPro; IPR013974; SAF.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR PANTHER; PTHR42966:SF3; BLR5971 PROTEIN; 1.
DR PANTHER; PTHR42966; N-ACETYLNEURAMINATE SYNTHASE; 1.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF03102; NeuB; 1.
DR Pfam; PF08666; SAF; 1.
DR SMART; SM00858; SAF; 1.
DR SUPFAM; SSF51269; AFP III-like domain; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF51658; Xylose isomerase-like; 1.
DR PROSITE; PS50844; AFP_LIKE; 1.
DR PROSITE; PS51371; CBS; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703}; Isomerase {ECO:0000256|ARBA:ARBA00023235}.
FT DOMAIN 3..63
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 404..462
FT /note="AFP-like"
FT /evidence="ECO:0000259|PROSITE:PS50844"
SQ SEQUENCE 747 AA; 82388 MW; 76214F66D67CF993 CRC64;
MIIERRLTPY LVFPEDSLLV ALQKMTDNRE RTVFVVDSHG FLVGSLTDGD VRRWRVAHPE
APLDVAAADV AHRDPATAPL GASPAEMREA LPTGARHLPL LDERGRLTAL AIDREAELCI
GGHRIGEGHP AFLIAEIGNN HQGDVDLARR LVDLAVEAGA DAVKFQLRDM DALYRQSGAA
TAGEDLGAQR TLDELAKFSL SAEDMVRVFD HVRDAGVALM CTPWDAPSMR VLRAYPVDGV
KIASADLTNH GLLRDAAASG LPMVLSTGMS REEEIRESVA LVRSFGVPFA MLHAQSTYPA
PYKDVNLAYL DRLAEIAQTP VGYSGHERGF HVALAAVARG AAIIEKHFTV DRGLEGNDHK
VSLLPEEFAQ MVRQTRDIEE SIGVGTERVV STGEAMNRIN LAKSLVAARP LQAGATITAD
DVTVKSPGRG LQPNELPRLV GRTLHREMAE GDFFFAGDLT DTVPTGRQFQ FRRPWGLPVR
YHDVAALTKD CTPDFLEFHF SYKDLEMDID SVFTEPLPMG FTTHLPDIFS GDFLVDLASD
DDAVWERSIA EVQRTIDITR DLKRWFPSEE APIMVITMGG FTLDRHIRPE ERQPKYERIA
EAVKRLDTSG IRIAAQTLPP FPWLMGGQQY HNLFMDPDDT VAFVEATGVP LCLDISHSKL
SATFLGIPFS EMVEKLAPHT IHLHLVDATG VDGEGPQIGE GDVDWPVLCE QLDRLAPGVS
FIPEIWQGHI NNGEGFWTAL DRLEQWL
//
