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Multifunctional fusion protein [Includes: N-acetylmuramic acid 6-phosphate etherase (MurNAc-6-P etherase) (EC 4.2.1.126) (N-acetylmuramic acid 6-phosphate hydrolase) (N-acetylmuramic acid 6-phosphate lyase); Anhydro-N-acetylmuramic acid kinase (EC 2.7.1.170) (AnhMurNAc kinase)]

 A0A1W9UAH4_9CHLR        Unreviewed;       685 AA.
A0A1W9UAH4;
05-JUL-2017, integrated into UniProtKB/TrEMBL.
05-JUL-2017, sequence version 1.
23-MAY-2018, entry version 7.
SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OQY18145.1};
Name=anmK {ECO:0000256|HAMAP-Rule:MF_01270};
Synonyms=murQ {ECO:0000256|HAMAP-Rule:MF_00068};
ORFNames=B6I35_13475 {ECO:0000313|EMBL:OQY18145.1};
Anaerolineaceae bacterium 4572_32.2.
Bacteria; Chloroflexi; Anaerolineae; Anaerolineales; Anaerolineaceae.
NCBI_TaxID=1971624 {ECO:0000313|EMBL:OQY18145.1, ECO:0000313|Proteomes:UP000192785};
[1] {ECO:0000313|Proteomes:UP000192785}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Dombrowski N., Seitz K., Teske A., Baker B.;
"Novel pathways for hydrocarbon cycling and metabolic
interdependencies in hydrothermal sediment communities.";
Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the specific phosphorylation of 1,6-anhydro-N-
acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of
the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the
utilization of anhMurNAc either imported from the medium or
derived from its own cell wall murein, and thus plays a role in
cell wall recycling. {ECO:0000256|HAMAP-Rule:MF_01270,
ECO:0000256|SAAS:SAAS00951629}.
-!- FUNCTION: Specifically catalyzes the cleavage of the D-lactyl
ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-
phosphate and D-lactate. {ECO:0000256|HAMAP-Rule:MF_00068,
ECO:0000256|SAAS:SAAS00767196}.
-!- CATALYTIC ACTIVITY: (R)-lactate + N-acetyl-D-glucosamine 6-
phosphate = N-acetylmuramate 6-phosphate + H(2)O.
{ECO:0000256|HAMAP-Rule:MF_00068, ECO:0000256|SAAS:SAAS00767175}.
-!- CATALYTIC ACTIVITY: ATP + 1,6-anhydro-N-acetyl-beta-muramate +
H(2)O = ADP + N-acetylmuramate 6-phosphate. {ECO:0000256|HAMAP-
Rule:MF_01270, ECO:0000256|SAAS:SAAS00951642}.
-!- PATHWAY: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate
degradation. {ECO:0000256|HAMAP-Rule:MF_01270,
ECO:0000256|SAAS:SAAS00951630}.
-!- PATHWAY: Amino-sugar metabolism; N-acetylmuramate degradation.
{ECO:0000256|HAMAP-Rule:MF_00068, ECO:0000256|SAAS:SAAS00767189}.
-!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
{ECO:0000256|HAMAP-Rule:MF_01270, ECO:0000256|SAAS:SAAS00951625}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00068,
ECO:0000256|SAAS:SAAS00767192}.
-!- MISCELLANEOUS: A lyase-type mechanism (elimination/hydration) is
suggested for the cleavage of the lactyl ether bond of MurNAc 6-
phosphate, with the formation of an alpha,beta-unsaturated
aldehyde intermediate with (E)-stereochemistry, followed by the
syn addition of water to give product. {ECO:0000256|HAMAP-
Rule:MF_00068}.
-!- SIMILARITY: Belongs to the GCKR-like family. MurNAc-6-P etherase
subfamily. {ECO:0000256|HAMAP-Rule:MF_00068,
ECO:0000256|SAAS:SAAS00767176}.
-!- SIMILARITY: Belongs to the anhydro-N-acetylmuramic acid kinase
family. {ECO:0000256|HAMAP-Rule:MF_01270,
ECO:0000256|SAAS:SAAS00951641}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:OQY18145.1}.
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EMBL; NBLW01000210; OQY18145.1; -; Genomic_DNA.
UniPathway; UPA00342; -.
UniPathway; UPA00343; -.
UniPathway; UPA00544; -.
Proteomes; UP000192785; Unassembled WGS sequence.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0016835; F:carbon-oxygen lyase activity; IEA:UniProtKB-UniRule.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:UniProtKB-UniRule.
GO; GO:0097175; P:1,6-anhydro-N-acetyl-beta-muramic acid catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
GO; GO:0097173; P:N-acetylmuramic acid catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniRule.
CDD; cd05007; SIS_Etherase; 1.
HAMAP; MF_01270; AnhMurNAc_kinase; 1.
HAMAP; MF_00068; MurQ; 1.
InterPro; IPR005338; Anhydro_N_Ac-Mur_kinase.
InterPro; IPR005488; Etherase_MurQ.
InterPro; IPR005486; Glucokinase_regulatory_CS.
InterPro; IPR001347; SIS.
PANTHER; PTHR30605; PTHR30605; 1.
Pfam; PF03702; AnmK; 1.
Pfam; PF01380; SIS; 1.
TIGRFAMs; TIGR00274; TIGR00274; 1.
PROSITE; PS01272; GCKR; 1.
PROSITE; PS51464; SIS; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01270,
ECO:0000256|SAAS:SAAS00951636};
Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00068,
ECO:0000256|SAAS:SAAS00767185};
Complete proteome {ECO:0000313|Proteomes:UP000192785};
Kinase {ECO:0000256|HAMAP-Rule:MF_01270,
ECO:0000256|SAAS:SAAS00951633};
Lyase {ECO:0000256|HAMAP-Rule:MF_00068,
ECO:0000256|SAAS:SAAS00767171};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01270,
ECO:0000256|SAAS:SAAS00951636};
Reference proteome {ECO:0000313|Proteomes:UP000192785};
Transferase {ECO:0000256|HAMAP-Rule:MF_01270,
ECO:0000256|SAAS:SAAS00951633}.
DOMAIN 437 600 SIS. {ECO:0000259|PROSITE:PS51464}.
NP_BIND 9 16 ATP. {ECO:0000256|HAMAP-Rule:MF_01270}.
ACT_SITE 465 465 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_00068}.
ACT_SITE 496 496 {ECO:0000256|HAMAP-Rule:MF_00068}.
SEQUENCE 685 AA; 71452 MW; 5BF8C6F764F89FF9 CRC64;
MIVIGLMSGT SADGIDAVVV ELQGAPPAIK WDLAAHTHVP HPPALRGEIF AAFEKGSAAQ
LCRLNVELGR AFGEAALQVI AAAKLTPAQV HLIGSHGQTI WHDPEAGATL QLGEAAVIAE
MTGSPVVSNF RPRDMAAGGQ GAPLVAYVDA LLFAHPRRVR SLQNIGGIAN LTYLPPSELG
PPPGLLAFDT GPGNALIDYA AGRATDGQWT FDRDGALAAQ GRISQELLDE LLAAPYLRQP
PPKTTGRELF GAQFGAQVWE QATARGLAPA DIVATLTAFT AHSIARAYRD FLPQPPAEVI
LSGGGARNLT LLAMLRERLP NVRVMLSDEL GVAAEAKEAL AFAVLAYETW HQRPGNLPAA
TGASRRVILG HITPGGRISE SANQRITNTT ESRNPATMDI DIVPTLEMAR LMNVEDRHVA
EAVAAELPQI AAAIDAIAAR MAQGGRLIYM GAGSSGRLGI LDAAECPPTF NTSPGQVVGL
IAGGESAITH AIEGAEDDAA AGAGEIAALN ISRQDSVVGI AASGRTPYVL GGLEQARQRG
ALTIGLVGNR ATAIENMADI TIAPVAGPEV IAGSTRLKAS TAQKMVLNML STGVMIRLGK
TFGNLMVDVQ ATNAKLRARA RRIVAQAAES AKGISEEEAG VLLERCNGQV KTAIVSILAE
LSPEEARRRL ATAGGIVRRA LRMDE


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